Binding of SHC1 to activated ERBB2 and the consequent RAS signaling activation is inhibited by the action of the PTPN12 protein tyrosine phosphatase. PTPN12 dephosphorylates tyrosine residue Y1248 of activated ERBB2 which serves as one of the docking sites for SHC1 in the ERBB2 C-terminus (Sun et al. 2011).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"Q05209-1"
],
"evidence": [
{
"id": "R-HSA-1963578",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963578"
}
]
},
{
"id": "R-HSA-1963581",
"name": "Trans-autophosphorylation of p-Y877-ERBB2 heterodimers",
"equation": "",
"summary": "Phosphorylation of ERBB2 on tyrosine residue Y877 by SRC family kinases significantly increases trans-autophosphorylation rate of ERBB2 heterodimers, presumably by enabling the kinase domain of ERBB2 to achieve a conformation that positively affects ERBB2 kinase activity. The downstream signaling of phosphorylated ERBB2 heterodimers that are phosphorylated on Y877 of ERBB2, in addition to the known trans-autophosphorylation sites, has not been studied extensively; it is assumed that the behavior of Y877-phosphorylated ERBB2 heterodimers is qualitatively similar to the behavior of trans-autophosphorylated ERBB2 heterodimers which do not harbor this modification.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-1963581",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963581"
}
]
},
{
"id": "R-HSA-1963582",
"name": "Trans-autophosphorylation of ERBB2 heterodimers",
"equation": "",
"summary": "Dimers of ERBB2 and EGF-bound EGFR trans-autophosphorylate on six EGFR tyrosine residues and six ERBB2 tyrosine residues to form phosphorylated heterodimers that activate downstream signaling cascades (Ricci et al. 1995, Pinkas-Kramarski et al. 1996, Walton et al. 1990, Margolis et al. 1989, Hazan et al. 1990, Helin et al. 1991).
In heterodimers of ERBB2 and neuregulin-stimulated ERBB3, ERBB2 phosphorylates ERBB3 on tyrosine residues that serve as docking sites for the p85 subunit of PI3K (Y1054, Y1197, Y1222, Y1224, Y1260, Y1276 and Y1289), as well as SHC1 (Y1328) and GRB7 (Y1199 and Y1262). Since ERBB3 lacks catalytic activity, it cannot phosphorylate ERBB2. Hovewer, since ERBB2:ERBB3 heterodimers usually oligomerize on the cell surface, ERBB2 can become trans-autophosphorylated by an adjacent ERBB2 protein. It is not known if ERBB2 in the ERBB2:ERBB3 hetero-oligomer is phosphorylated on all conserved tyrosine residues and if the phosphorylation status of ERBB2 in the ERBB2:ERBB3 hetero-oligomer significantly affects signaling (Li et al. 2007, Pinkas-Kramarski et al. 1996, Prigent et al. 1994, Vijapurkar et al. 2003, Wallasch et al. 1995).
Heterodimers of ERBB2 and ERBB4 trans-autophosphorylate on tyrosine residues that serve as docking sites for PLC-gamma, GRB2 and SHC1, as well as p85 subunit of PI3K (PIK3R1) in the case of ERBB2 heterodimers with ERBB4 CYT1 isoforms (ERBB4cyt1) - ERBB4 JM-A CYT1 and ERBB4 JM-B-CYT1 (Li et al. 2007, Kaushansky et al. 2008, Hazan et al. 1990, Cohen et al. 1996).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-1963582",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963582"
}
]
},
{
"id": "R-HSA-1963586",
"name": "SRC family kinases phosphorylate ERBB2",
"equation": "",
"summary": "Dissociation of HSP90 from ERBB2 upon formation of ERBB2 heterodimers (with either EGFR, ERBB3 or ERBB4) enables phosphorylation of ERBB2 on the tyrosine residue Y877, mediated by one of SRC family kinases - SRC, FYN or YES1. Although not a mandatory prerequisite of ERBB2 catalytic activity, the phosphorylation at Y877 significantly increases the kinase activity of ERBB2.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P06241-1",
"P12931-1",
"P07947-1"
],
"evidence": [
{
"id": "R-HSA-1963586",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963586"
}
]
},
{
"id": "R-HSA-1963589",
"name": "ERBB2 forms heterodimers with ligand-activated ERBB receptors: EGFR, ERBB3 and ERBB4",
"equation": "",
"summary": "ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member. ERBB2 heterodimerization partners are EGF-stimulated EGFR (Wada et al. 1990, Karunagaran et al. 1996), ERBB3 stimulated by neuregulins NRG1 or NRG2 (Pinkas-Kramarski et al. 1996), and ERBB4 stimulated by neuregulins or EGF-like ligands (Li et al. 2007). In the process of dimerization, ERBB2 dissociates from chaperone proteins HSP90 and CDC37 (Xu et al 2001, Citri et al. 2004). Activated ERBB2 also dissociates from ERBB2IP, the protein responsible for proper localization of ERBB2 to basolateral membranes of epithelial cells (Borg et al. 2000).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-1963589",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963589"
}
]
},
{
"id": "R-HSA-1977959",
"name": "ERBB4 forms heterodimers with EGFR",
"equation": "",
"summary": "Ligand-stimulated ERBB4 was shown to form heterodimers with ligand-stimulated EGFR when human ERBB4 and EGFR were exogenously expressed in mouse fibroblast cell line. Heterodimers of ERBB4 and EGFR undergo trans-autophosphorylation, but the exact phosphorylation pattern, downstream signaling and physiological significance of these heterodimers have not been studied (Riese et al. 1995, Cohen et al. 1996). Binding of ERBB4 CYT2 isoform to EGFR protects EGFR from ligand-induced degradation by preventing binding of the CBL:GRB2 complex to EGFR (Kiuchi et al. 2014).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-1977959",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1977959"
}
]
},
{
"id": "R-HSA-212706",
"name": "Phospholipase C-gamma1 binds to the activated EGF receptor",
"equation": "",
"summary": "Inactive phospholipase C-gamma1 (PLCG1) binds to activated epidermal growth factor receptor (EGFR).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-212706",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-212706"
}
]
},
{
"id": "R-HSA-212710",
"name": "EGFR activates PLC-gamma1 by phosphorylation",
"equation": "",
"summary": "EGFR phosphorylates PLC-gamma1, thus activating it.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-212710",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-212710"
}
]
},
{
"id": "R-HSA-212713",
"name": "Active PLC-gamma1 dissociates from EGFR",
"equation": "",
"summary": "Once activated PLC-gamma1 dissociates from EGFR, it can hydrolyze PIP2.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-212713",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-212713"
}
]
},
{
"id": "R-HSA-2179387",
"name": "Mature HBEGF binds to EGFR, triggering dimerisation and autophosphorylation of the receptor",
"equation": "",
"summary": "The heparin-binding EGF growth factor (HBEGF) is a member of the EGF family of growth factors that binds to and activates the EGF receptor EGFR/ErbB1 and ErbB4 (not shown here) (Higashiyama et al. 1991, Elenius et al. 1997). The details which describe receptor dimerisation on ligand binding and autophosphorylation from experiments in mice have been omitted here.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-2179387",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2179387"
}
]
},
{
"id": "R-HSA-2179407",
"name": "SOS1-mediated nucleotide exchange of RAS (HB-EFG-initiated)",
"equation": "",
"summary": "SOS1 is the guanine nucleotide exchange factor (GEF) for RAS. SOS1 activates RAS nucleotide exchange from the inactive form (bound to GDP) to an active form (bound to GTP) (Chardin et al. 1993).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-2179407",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2179407"
}
]
},
{
"id": "R-HSA-2179415",
"name": "GRB2:SOS1 binds to HBEGF:p-Y-EGFR",
"equation": "",
"summary": "Cytoplasmic target proteins containing the SH2 domain can bind to activated EGFR. One such protein, growth factor receptor-bound protein 2 (GRB2), can bind activated EGFR with its SH2 domain whilst in complex with SOS through its SH3 domain. GRB2 can bind at either Y1068 and/or Y1086 autophosphorylation sites on the receptor (Batzer et al. 1994, Okutani et al. 1994).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-2179415",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2179415"
}
]
},
{
"id": "R-HSA-2316434",
"name": "PI3K phosphorylates PIP2 to PIP3",
"equation": "",
"summary": "A number of different extracellular signals converge on PI3K activation. PI3K can be activated downstream of receptor tyrosine kinases (RTKs) such as FGFR (Ong et al. 2001, Eswarakumar et al. 2005), KIT (Chian et al. 2001, Ronnstrand 2004, Reber et al. 2006), PDGF (Coughlin et al. 1989, Fantl et al. 1992, Heldin et al. 1998), insulin receptor IGF1R (Hadari et al. 1992, Kooijman et al. 1995), and EGFR and its family members (Rodrigues et al. 2000, Jackson et al. 2004, Kainulainen et al. 2000, Junttila et al. 2009). Other proteins, such as CD28 (Pages et al. 1996, Koyasu 2003, Kane and Weiss, 2003) and TRAT1 (Bruyns et al. 1998, Koyasu 2003, Kolsch et al. 2006), can also trigger PI3K activity.
In unstimulated cells, PI3K class IA exists as an inactive heterodimer of a p85 regulatory subunit (encoded by PIK3R1, PIK3R2 or PIK3R3) and a p110 catalytic subunit (encoded by PIK3CA, PIK3CB or PIK3CD). Binding of the iSH2 domain of the p85 regulatory subunit to the ABD and C2 domains of the p110 catalytic subunit both stabilizes p110 and inhibits its catalytic activity. This inhibition is relieved when the SH2 domains of p85 bind phosphorylated tyrosines on activated RTKs or their adaptor proteins. Binding to membrane-associated receptors brings activated PI3K in proximity to its membrane-localized substrate, PIP2 (Mandelker et al. 2009, Burke et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22455-1",
"P16234-1",
"P42336-1",
"Q9NWZ3-1",
"P00533-1",
"P04626-1",
"P06241-1",
"P10721-1",
"P12931-1",
"P63000-1",
"P06239-1",
"Q06124-2",
"Q9Y4K3-1",
"P36888-1",
"P09619-1",
"P42338-1",
"O00329-1",
"P08581-1",
"Q01638-1",
"P51617-1"
],
"evidence": [
{
"id": "R-HSA-2316434",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2316434"
}
]
},
{
"id": "R-HSA-2400009",
"name": "PI3K inhibitors block PI3K catalytic activity",
"equation": "",
"summary": "A variety of inhibitors capable of blocking the phosphoinositide kinase activity of PI3K have been developed. These inhibitors display differential selectivity and inhibit kinase activity of their substrates by distinct mechanisms. For example, the first-generation PI3K inhibitor wortmannin (Wymann et al. 1996) covalently and irreversibly binds all classes of PI3K enzymes, as well as other kinases including mTOR, at a residue critical for catalytic activity. Although wortmannin is precluded from in vivo and clinical use due to its toxicity, it has proven to be a useful tool for in vitro laboratory studies. Newer inhibitors, such as BEZ235, are currently being investigated in Phase I clinical trials. BEZ235 is a dual pan-class I PI3K/mTOR inhibitor that blocks kinase activity by binding competitively to the ATP-binding pocket of these enzymes (Serra et al. 2008, Maira et al. 2008). BGT226 (Chang et al. 2011) and XL765 (Prasad et al. 2011) also inhibits both PI3K class I enzymes and mTOR. Other inhibitors in clinical trials, such as BKM120 (Maira et al. 2012), GDC0941 (Folkes et al. 2008, Junttila et al. 2009) and XL147 (Chakrabarty et al. 2012), are specific for class I PI3Ks and exhibit no activity against mTOR. Current research aims to identify isoform-specific PI3K inhibitors. Small molecule inhibitors that selectively inhibit PIK3CA (p110alpha), e.g. PIK-75 and A66, were used to study the role of p110alpha in signaling and growth of tumor cells (Knight et al. 2006, Sun et al. 2010, Jamieson et al. 2011, Utermark et al. 2012). The PIK3CB (p110beta) specific inhibitor TGX221 has been used in in vitro models of vascular injury (Jackson et al. 2005), and the TGX221 derivative KIN-193 has been shown to block AKT activity and tumor growth in mice with p110beta activation or PTEN loss (Ni et al. 2012). CAL-101 is a PIK3CD (p110delta) specific inhibitor that is being clinically investigated as a therapeutic for lymphoid malignancies (Herman et al. 2010). It is hoped that, in the future, more specific inhibitors, such as those targeting selective PI3K isoforms, will provide optimum treatment while minimizing unwanted side effects. For a recent review, please refer to Liu et al. 2009.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22455-1",
"P16234-1",
"P42336-1",
"P00533-1",
"P04626-1",
"P06241-1",
"P10721-1",
"P12931-1",
"P63000-1",
"P06239-1",
"Q06124-2",
"P36888-1",
"P09619-1",
"P42338-1",
"O00329-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-2400009",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2400009"
}
]
},
{
"id": "R-HSA-445069",
"name": "L1-EGFR trans-heterodimerization",
"equation": "",
"summary": "L1CAM and EGFR engage in a weak heterophilic trans interaction and this induces EGFR tyrosine kinase activity and its activation. However, this trans interaction alone is not sufficient to induce EGFR autophosphorylation, which requires additional cis type interactions between the two proteins.",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-179837",
"R-HSA-191465"
],
"output_participant_list": [
"R-HSA-179837"
],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-445069",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-445069"
}
]
},
{
"id": "R-HSA-5637764",
"name": "Binding of GRB2:GAB1 complex to p-EGFRvIII mutant",
"equation": "",
"summary": "Direct binding of the GRB2:GAB1 complex to phosphorylated homodimers of EGFRvIII cancer mutant has not been tested. This complex is recruted to EGFR via GRB2 binding to phosphorylated tyrosine residues Y1068 and Y1086 (corresponding to Y1092 and Y1110, respectively, when counting from the first amino acid of the EGFR precursor, prior to cleavage of the 24-amino acid signal peptide at the N-terminus). Phosphorylation of Y1068 (i.e. Y1092) has been directly demonstrated in EGFRvIII mutant (Huang et al. 2007).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637764",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637764"
}
]
},
{
"id": "R-HSA-5637765",
"name": "Binding of PI3K to complex of GRB2:GAB1 and p-EGFRvIII",
"equation": "",
"summary": "EGFRvIII cancer mutant is assumed to recruit the PI3K complex PIK3CA:PIK3R1 in a manner similar to wild-type EGFR (Rodrigues et al. 2000).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637765",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637765"
}
]
},
{
"id": "R-HSA-5637766",
"name": "Binding of SHC1 to p-5Y-EGFRvIII",
"equation": "",
"summary": "SHC1 (Src homology 2 domain-containing transforming protein) is known to bind two phosphorylated tyrosine docking sites of EGFR: Y1148 and Y1173 (corresponding to Y1172 and Y1197 when counting from the first amino acid of EGFR precursor, before the cleavage of the 24-amino acid signal peptide at the N-terminus takes place). Phosphorylation of Y1173 tyrosine residue was directly demonstrated in EGFRvIII mutant (Han et al. 2006, Grandal et al. 2007) as well as the phosphorylation of Y1148 (Huang et al. 2007).
Binding of SHC1 to EGFRvIII cancer mutant has not been tested but SHC1 is assumed to bind EGFRvIII in the same way it binds wild-type EGFR.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637766",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637766"
}
]
},
{
"id": "R-HSA-5637770",
"name": "Binding of GRB2:SOS1 complex to phosphorylated EGFRvIII",
"equation": "",
"summary": "Direct binding of GRB2:SOS1 complex to phosphorylated homodimers of EGFRvIII cancer mutant has not been tested. GRB2 binds to phosphorylated tyrosine residues Y1068 and Y1086 (corresponding to Y1092 and Y1110, respectively, when counting from the first amino acid of the EGFR precursor, prior to cleavage of the 24-amino acid signal peptide at the N-terminus). Phosphorylation of Y1068 (i.e. Y1092) has been directly demonstrated in EGFRvIII mutant (Huang et al. 2007).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637770",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637770"
}
]
},
{
"id": "R-HSA-5637792",
"name": "PLC-gamma 1 binds to p-EGFRvIII mutant",
"equation": "",
"summary": "Tyrosine residue Y992 (corresponding to Y1016 when counting from the first amino acid of the EGFR precursor, prior to cleavage of the 24-amino acid signal peptide at the N-terminus), a docking site for PLC-gamma 1 (PLCG1), is phosphorylated in EGFRvIII cancer mutant and expected to recruit PLC-gamma 1 in the same way as the wild-type EGFR receptor (Grandal et al. 2007).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P19174-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637792",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637792"
}
]
},
{
"id": "R-HSA-5637794",
"name": "EGFRvIII does not bind CBL",
"equation": "",
"summary": "In EGFRvIII mutant, Y1069 (i.e. Y1045 in the mature protein) is not phosphorylated (Han et al. 2006, Grandal et al. 2007). Han et al. detected no CBL binding to EGFRvIII mutant (Han et al. 2006), while Grandal et al. detected very little binding, which they explained by indirect recruitment of CBL to EGFRvIII through GRB2 (Grandal et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P22681-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637794",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637794"
}
]
},
{
"id": "R-HSA-5637795",
"name": "Phosphorylation of PLC-gamma 1 by p-EGFRvIII mutant",
"equation": "",
"summary": "Once recruited, PLC-gamma 1 is assumed to be phosphorylated by EGFRvIII cancer mutant in the same way it is phosphorylated by the wild-type EGFR (Meisenhelder et al. 1989, Wahl et al. 1990).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P19174-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637795",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637795"
}
]
},
{
"id": "R-HSA-5637796",
"name": "Phosphorylation of SHC1 by p-5Y-EGFRvIII",
"equation": "",
"summary": "EGFRvIII cancer mutant was not directly tested for its ability to phosphorylate SHC1, but is assumed to interact with SHC1 in the same way as the wild-type EGFR protein (Soler et al. 1994, VanderKuur et al. 1995).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637796",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637796"
}
]
},
{
"id": "R-HSA-5637798",
"name": "Phosphorylated SHC1 in complex with p-5Y-EGFRvIII recruits GRB2:SOS1 complex",
"equation": "",
"summary": "Recruitment of GRB2:SOS1 complex by SHC1 bound to phosphorylated dimers of EGFRvIII cancer mutant has not been directly tested, but is assumed to happen in the same way it happens with the SHC1 bound to the phosphorylated homodimer of wild-type EGFR (Chardin et al. 1993).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637798",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637798"
}
]
},
{
"id": "R-HSA-5637800",
"name": "Dissociation of phosphorylated PLC-gamma 1 from p-EGFRvIII mutant",
"equation": "",
"summary": "Once phosphorylated, PLC-gamma 1 is expected to dissociate from phosphorylated EGFRvIII cancer mutant and induce downstream signaling in the same way it does when activated by the wild-type EGFR. However, except for the phosphorylation of PLCG1 binding site in EGFRvIII (Grandal et al. 2007), other events involved in activation of PLCG1 signaling have not been studied in cells expressing EGFRvIII.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P19174-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637800",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637800"
}
]
},
{
"id": "R-HSA-5637801",
"name": "Conversion of PIP2 to PIP3 by PI3K bound to phosphorylated EGFRvIII",
"equation": "",
"summary": "The kinase activity of PI3K mediates the phosphorylation of PIP2 to form PIP3. It is assumed that EGFRvIII cancer mutant induces PI3K/AKT signaling in a manner similar to wild-type EGFR. Accordingly, activation of PI3K/AKT signaling cascade has been demonstrated in cells expressing EGFRvIII (Lammering et al. 2003, Li et al. 2004)",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637801",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637801"
}
]
},
{
"id": "R-HSA-5637806",
"name": "SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with p-EGFRvIII)",
"equation": "",
"summary": "Based on the wild-type EGFR signaling, it is assumed that the guanine nucleotide exchange factor SOS1 interacts with phosphorylated EGFRvIII mutant through the adaptor protein, GRB2. Upon formation of this complex, SOS1 activates RAS by promoting GDP release and GTP binding. Although this reaction has not been directly confirmed for EGFRvIII cancer mutant, RAS-MAPK signaling cascade is activated in cells expressing EGFRvIII (Montgomery et al.1995).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P07900-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-5637806",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637806"
}
]
},
{
"id": "R-HSA-5637808",
"name": "SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with phosphorylated SHC1 and p-EGFRvIII)",
"equation": "",
"summary": "SOS1 is the guanine nucleotide exchange factor (GEF) for RAS. SOS1, recruited by GRB2 bound to p-SHC1:p-EGFRvIII mutant, is assumed to activate RAS nucleotide exchange from the inactive form (bound to GDP) to an active form (bound to GTP). Although this reaction has not been shown to occur directly for EGFRvIII cancer mutant, activation of RAF/MAP kinase cascade has been demonstrated in cells expressing EGFRvIII (Montgomery et al. 1995).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P07900-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-5637808",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637808"
}
]
},
{
"id": "R-HSA-5638137",
"name": "EGFRvIII cancer variant does not bind EGF ligand",
"equation": "",
"summary": "EGFRvIII mutant lacks the ligand binding domain and is therefore unable to bind EGFR ligands (Fernandes et al. 2001).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5638137",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5638137"
}
]
},
{
"id": "R-HSA-5672965",
"name": "RAS GEFs promote RAS nucleotide exchange",
"equation": "",
"summary": "The human genome is predicted to encode 27 RAS guanine nucleotide exchange factors (GEFs) that promote the exchange of GDP for GTP on membrane-associated RAS in response to RAS-MAPK pathway activation by growth factors, hormones, cytokines and other stimuli (reviewed in Cherfils and Zeghouf, 2013; Cargnello and Roux, 2011). Nucleotide exchange stimulates a conformational change in RAS to facilitate its interaction with RAF, ultimately promoting the phosphorylation of downstream effectors MAPK3 and MAPK1 (also known as ERK1 and ERK2) (reviewed in Cseh et al, 2014; Vigil et al, 2010).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P07949-1",
"P22455-1",
"P52333-1",
"P16234-1",
"O60674-1",
"Q9UQM7-1",
"P00533-1",
"P04626-1",
"P06241-1",
"P10721-1",
"Q13554-1",
"Q02763-1",
"P01112-1",
"P36888-1",
"P09619-1",
"P18433-5",
"Q05397-1",
"Q13557-1",
"P08581-1",
"P23458-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-5672965",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5672965"
}
]
},
{
"id": "R-HSA-6785636",
"name": "Phosphorylated ERBB2 heterodimers bind MEMO1",
"equation": "",
"summary": "ERBB2 phosphorylated on tyrosine residue Y1222 binds MEMO1 (mediator of ERBB2-driven cell motility) (Marone et al. 2004, Qiu et al. 2008, Zaoui et al. 2010, Feracci et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-6785636",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6785636"
}
]
},
{
"id": "R-HSA-6785648",
"name": "MEMO1 binds RHOA:GTP:DIAPH1",
"equation": "",
"summary": "MEMO1, in complex with phosphorylated ERBB2 heterodimers, associates with the complex of activated RHOA and formin family member DIAPH1. MEMO1 maintains the plasma membrane association of the RHOA:GTP:DIAPH1 complex (Zaoui et al. 2008) and modulates RHOA:GTP:DIAPH1-regulated actin and microtubule dynamics and the consequent cell motility/migration downstream of ERBB2 (Marone et al. 2004, Zaoui et al. 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P61586-1"
],
"evidence": [
{
"id": "R-HSA-6785648",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6785648"
}
]
},
{
"id": "R-HSA-8847995",
"name": "Activated ERBB2 binds PTK6 (BRK)",
"equation": "",
"summary": "PTK6 (BRK) is a nonreceptor tyrosine kinase that can bind activated ERBB2 receptor (Xiang et al. 2008).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13882-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-8847995",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8847995"
}
]
},
{
"id": "R-HSA-8848005",
"name": "ERBB2 promotes PTK6 autophosphorylation",
"equation": "",
"summary": "Binding of PTK6 (BRK) to activated ERBB2 receptor stimulates autophosphorylation of PTK6 on tyrosine residue Y342 (Xiang et al. 2008, Peng et al. 2015). Autophosphorylation at Y342 significantly increases catalytic activity of PTK6 (Qiu and Miller 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-8848007"
],
"enzyme_list": [
"Q13882-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-8848005",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8848005"
}
]
},
{
"id": "R-HSA-8857549",
"name": "HBEGF-bound EGFR forms a heterodimer with GPNMB",
"equation": "",
"summary": "EGFR bound to HBEGF (HB-EGF) can form heterodimers with the transmembrane glycoprotein GPNBM. The intracellular domain of GPNMB interacts with the kinase domain of EGFR (Lin et al. 2016).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-8857549",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8857549"
}
]
},
{
"id": "R-HSA-8857555",
"name": "EGFR phosphorylates GPNMB",
"equation": "",
"summary": "HBEGF-bound EGFR phosphorylates its heterodimerization partner GPNMB at tyrosine residue Y525 (Lin et al. 2016). It is not clear whether trans-autophosphorylation of HBEGF-bound EGFR homodimers precedes heterodimerization of EGFR with GPNBM and GPNMB phosphorylation or if the interaction of GPNMB with the kinase domain of EGFR is sufficient for EGFR kinase activation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-8857555",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8857555"
}
]
},
{
"id": "R-HSA-8857565",
"name": "Phosphorylated GPNMB recruits PTK6 and LRRK2 in the presence of LINC01139",
"equation": "",
"summary": "Phosphorylation of GPNBM at tyrosine residue Y525 upon heterodimerization with HBEGF-bound EGFR promotes, in the presence of long non-coding RNA LINC011139 (LINK-A), the recruitment of PTK6 (BRK). In addition to PTK6, LINC01139 simultaneously recruits serine/threonine kinase LRRK2 to phosphorylated GPNBM (Lin et al. 2016).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13882-1",
"P00533-1",
"Q5S007-1"
],
"evidence": [
{
"id": "R-HSA-8857565",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8857565"
}
]
},
{
"id": "R-HSA-8857577",
"name": "LINC01139 facilitates PTK6 autophosphorylation",
"equation": "",
"summary": "The long non-coding RNA LINC01139 (LINK-A) induces conformational change of PTK6 (BRK), which facilitates PTK6 autophosphorylation on tyrosine residue Y351 and possibly other sites (Lin et al. 2016).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13882-1",
"P00533-1",
"Q5S007-1"
],
"evidence": [
{
"id": "R-HSA-8857577",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8857577"
}
]
},
{
"id": "R-HSA-8857583",
"name": "LINC01139 promotes phosphorylation of HIF1A by PTK6",
"equation": "",
"summary": "PTK6 (BRK) tyrosine kinase, activated via long non-coding RNA LINC01139 (LINK-A) mediated recruitment to phosphorylated GPNMB (bound to HBEGF-activated EGFR), phosphorylates hypoxia inducible factor 1 alpha (HIF1A) at tyrosine residue Y565. Phosphorylation of HIF1A by PTK6 at Y565 inhibits HIF1A hydroxylation at proline P564, resulting in HIF1A stabilization under normoxic conditions (Lin et al. 2016).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13882-1",
"P00533-1",
"Q5S007-1"
],
"evidence": [
{
"id": "R-HSA-8857583",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8857583"
}
]
},
{
"id": "R-HSA-8857925",
"name": "Inhibition of PP2A activity by phosphorylation of the catalytic subunit at tyrosine Y307",
"equation": "",
"summary": "SRC family tyrosine kinases, such as SRC and LCK, as well as receptor tyrosine kinases, such as EGFR and insulin receptor, can phosphorylate the catalytic subunit of serine/threonine protein phosphatase PP2A at tyrosine residue Y307. Phosphorylation at Y307 inhibits the catalytic activity of PP2A. Phosphatidylinositol-5-phosphate (PI5P) positively regulates phosphorylation of the catalytic subunit of PP2A at Y307.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P67775-1",
"P06239-1",
"P06213-1",
"P62714-1"
],
"evidence": [
{
"id": "R-HSA-8857925",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8857925"
}
]
},
{
"id": "R-HSA-8863804",
"name": "PTPN12 dephosphorylates ERBB2 on tyrosine Y1248",
"equation": "",
"summary": "PTPN12 protein tyrosine phosphatase dephosphorylates activated ERBB2 at tyrosine residue Y1248 and activated EGFR at tyrosine residue Y1148 (Y1148 corresponds to Y1172 of the nascent EGFR, with 24 amino acid signal peptide at the N-terminus). PTPN12-mediated dephosphorylation of ERBB2 attenuates downstream RAS activation, as Y1248 is involved in SHC1 recruitment. Similar to Y1148 of EGFR, Y1248 of ERBB2 is part of the NPXY motif that is, when phosphorylated on the tyrosine residue, recognized by the N-terminal phosphotyrosine interaction domain (PID) of SHC1 (Batzer et al. 1995, Songyang et al. 1995). SHC1 itself could be a target for PTPN12. PTPN12 function is frequently lost in triple negative breast cancer (Sun et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"Q05209-1"
],
"evidence": [
{
"id": "R-HSA-8863804",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8863804"
}
]
},
{
"id": "R-HSA-8864029",
"name": "PTPN12 dephosphorylates EGFR at Y1172 (Y1148)",
"equation": "",
"summary": "PTPN12 protein tyrosine phosphatase dephosphorylates activated EGFR at tyrosine residue Y1148 (Y1148 corresponds to Y1172 in the nascent EGFR sequence which includes the 24 amino acid long signal peptide at the N-terminus). PTPN12-mediated dephosphorylation of activated EGFR inhibits SHC1 recruitment to the p-Y1148 (i.e. p-Y1172) docking site, thus attenuating downstream RAS activation (Sun et al. 2011). The recruitment of SHC1 to p-Y1148 (i.e. Y1172) of EGFR is mediated by the N-terminal phosphotyrosine interaction domain (PID) of SHC1 (Batzer et al. 1995, Songyang et al. 1995).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"Q05209-1"
],
"evidence": [
{
"id": "R-HSA-8864029",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8864029"
}
]
},
{
"id": "R-HSA-8864105",
"name": "PTPN18 binds ERBB2:EGFR heterodimers",
"equation": "",
"summary": "PTPN18 protein tyrosine phosphatase (BDP1) binds ERBB2, activated in response to EGF stimulation, via PEST and catalytic domains of PTPN18 (Wang et al. 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"Q99952-1"
],
"evidence": [
{
"id": "R-HSA-8864105",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8864105"
}
]
},
{
"id": "R-HSA-8864125",
"name": "PTPN18 dephosphorylates ERBB2 at Y1196, Y1112 and Y1248",
"equation": "",
"summary": "Protein tyrosine kinase PTPN18 dephosphorylates ERBB2, activated in response to EGF stimulation (Gensler et al. 2004), at tyrosine residues Y1196, Y1112 and Y1248 (Wang et al. 2014). PTPN18 does not dephosphorylate activated EGFR. Dephosphorylation of ERBB2 tyrosines Y1196 and Y1248 attenuates downstream activation of PI3K/AKT and RAS signaling. Dephosphorylation of Y1112 interferes with the recruitment of CBL E3 ubiquitin ligase to activated ERBB2 and CBL-mediated lysosomal route of ERBB2 down-regulation. When phosphorylated by an unknown serine/threonine kinase in an AKT-dependent manner on serine residues S419 and S423, PTPN18 recruits beta-TRCP ubiquitin ligase complex to ERBB2, thus promoting proteasome-dependent ERBB2 degradation (Wang et al. 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"Q99952-1"
],
"evidence": [
{
"id": "R-HSA-8864125",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8864125"
}
]
},
{
"id": "R-HSA-8866279",
"name": "Epsin family proteins bind ubiquitinated cargo",
"equation": "",
"summary": "Some membrane cargo is sorted into clathrin-coated pits after ubiquitination of the cytosolic domain (reviewed in Piper et al 2014). Ubiquitinated cargo is recognized by adaptor proteins such as EPS15, EPN1 and EPN2 that contain ubiquitin-binding domains and also interact with components of the clathrin coat (Chen et al, 1998; Rosenthal et al, 1999; Polo et al, 2002; Shih et al, 2002; Haglund et al, 2003; Schmid et al, 2006; reviewed in Sen et al, 2012; Piper et al, 2014). A number of receptor tyrosine kinases, including EGFR, VEGFR, FGFR and others undergo ubiquitination at the plasma membrane, triggering endocytosis. Internalized RTKs can undergo recycling or degradation, the latter of which serves to terminate signaling (reviewed in Sorkin and von Zastrow, 2009; Haglund and Dikic, 2012). Ubiquitin-based sorting into CCPs appears to be dynamic as deubiquitinases have been identified as components of some CCPs (Weinberg and Drubin, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P22681-1"
],
"evidence": [
{
"id": "R-HSA-8866279",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8866279"
}
]
},
{
"id": "R-HSA-8867041",
"name": "EGFR phosphorylates EPS15",
"equation": "",
"summary": "EPS15 is phosphorylated at Y849 by activated EGFR (Confalonieri et al, 2000). While the roles of phosphorylation and ubiquitination in EGFR endocytosis are unclear, emerging evidence suggests that EPS15 phosphorylation may target the activated EGFR complex for endocytosis through a clathrin-mediated route, while dephosphorylation at Y849 may direct the receptor complex into a clathrin-independent route (Confalonieri et al, 2002; de Melker et al, 2004; Li et al, 2015; reviewed in van Bergen en Henegouwen, 2009).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P22681-1"
],
"evidence": [
{
"id": "R-HSA-8867041",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8867041"
}
]
},
{
"id": "R-HSA-8867044",
"name": "EGFR binds EPS15, EPN1, EPS15L1",
"equation": "",
"summary": "EH-containing proteins such as EPS15, EPN1 and EPS15L1 are required for the endocytosis of ligand-activated EGFR (Confalonieri et al, 2000; Huang et al, 2004; reviewed in van Bergen en Henegouwen, 2009). EPS15 and EPN1 bind components of the clathrin coated pit through DPF motifs and likely bind to EGFR through the ubiquitin interacting motifs (UIMs). In this way EH proteins may help cluster activated EGFR into nascent clathrin-coated pits (Kazazic et al, 2009; Benmerah et al, 2000; reviewed in van Bergen en Henegouwen, 2009). Note, however, that EH-containing proteins are also involved in the clathrin-independent endocytosis of EGFR (Sigismund et al, 2005)",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P22681-1"
],
"evidence": [
{
"id": "R-HSA-8867044",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8867044"
}
]
},
{
"id": "R-HSA-8867047",
"name": "PTPN3 dephosphorylates EPS15",
"equation": "",
"summary": "While the roles of EGFR and EPS15 phosphorylation and ubiquitination are not completely clear, recent evidence supports the idea that EGFR-mediated phosphorylation of EPS15 promotes the clustering of the activated receptor into clathrin-coated pits, while the dephosphorylated EPS15 targets EGFR for endocytosis through a caveolin-and lipid raft-dependent route (reviewed in van Bergen en Henegouwen, 2009). Consistent with this, overexpression of the phosphatase PTPN3, which dephosphorylates EPS15 in vitro and in vivo, promotes the internalization of EGFR into caveolin-enriched structures and targets it for lysosomal degradation (Li et al, 2015).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P22681-1",
"P26045-1"
],
"evidence": [
{
"id": "R-HSA-8867047",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8867047"
}
]
},
{
"id": "R-HSA-8867754",
"name": "F- and N- BAR domain proteins bind the clathrin-coated pit",
"equation": "",
"summary": "BAR (BIN/amphiphysin/Rvs) domain proteins sense and contribute to membrane curvature. BAR domain proteins generally form long, coiled-coil homo- or hetero-dimers with a concave inner surface that interacts with membranes (reviewed in Gallop and McMahon, 2005; Daumke et al, 2014). F-BAR domain proteins such as FCHo 1 and 2 recognize shallow membrane curvature and are generally recruited early in the formation of clathrin-coated pit (Itoh et al, 2005; Kamioka et al, 2004; Henne et al, 2007; Shimada et al, 2007; Henne et al, 2010). FNBP proteins and N-BAR containing endocytic proteins such as SNX9 and 18, amphiphysin (AMPH) and endophilins recognize regions of membrane with greater curvature, interact with dynamin and likely play a later role in CCP formation with spatiotemporal coupling to vesicle scission (Kamioka et al, 2004; Itoh et al, 2005; Soulet et al, 2005; Shimada et al, 2007; Shin et al, 2008; Taylor et al, 2011; reveiwed in McMahon and Boucrot, 2011). These proteins are recruited to the complex through interactions with core components of the clathrin-coated pit, and in the case of SNX9, also through interaction with PI(3,4)P2, which is generated at late stages by clathrin-associated PIK3C2A (Lundmark and Carlson, 2003; Schmid et al, 2006; Dergai et al, 2010; Brett et al, 2002 : Posor et al, 2013; reviewed in Daumke et al, 2014). Early BAR domain containing proteins such as FCHo1 and 2 are not present in either late stage clathrin-coated pits or in free clathrin-coated vesicles. Although the precise timing of their dissociation is not known, in this pathway, they are shown leaving the clathrin-coated pit upon recruitment of the more highly curved N-BAR proteins (Taylor et al, 2011).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O00443-1",
"P00533-1",
"P22681-1",
"Q2M2I8-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-8867754",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8867754"
}
]
},
{
"id": "R-HSA-8867756",
"name": "CLASP proteins and cargo are recruited to the nascent clathrin-coated pit",
"equation": "",
"summary": "CLASP proteins are recruited to nascent clathrin-coated pits (CCPs) through interactions with AP-2 and clathrin. Although in this pathway cargo recruitment is depicted as occuring after the recruitment of bulk AP-2 and clathrin, a number of studies suggest that they are largely recruited concomitantly (Liu et al, 2010; reviewed in McMahon and Boucrot, 2011). Concurrent interactions with sorting signals in cargo cytoplasmic tails and with clathrin and/or AP-2 ensure that CLASPs and cargo are incorporated into the emerging CCP (Schmid et al, 2006; Edeling et al, 2006; reviewed in Traub, 2009; Traub and Bonifacino, 2013; Kirchausen et al, 2014). In addition, incorporation of CLASPs and cargo may play a role in regulating the timing and dynamics of endocytosis (Loerke et al, 2009; Mettlen et al, 2009; Soohoo et al, 2013; Mettlen et al, 2010; Puthenveedu et al, 2005).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P22681-1",
"Q2M2I8-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-8867756",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8867756"
}
]
},
{
"id": "R-HSA-8868071",
"name": "Clathrin recruits PIK3C2A",
"equation": "",
"summary": "PIK3C2A is a member of the class II PI 3 kinases, and phosphorylates PI(4)P to PI(3,4)P2 at the plasma membrane. PIK3C2A interacts with clathrin through a clathrin-binding domain in its unique N-terminal tail and localizes to late-stage clathrin-coated pits (Domin et al, 2000; Gaidarov et al, 2001; Gaidarov et al, 2005). Binding to clathrin stimulates the kinase activity of PIK3C2A and promotes the production of PI(3,4)P2 at the plasma membrane (Gaidarov et al, 2001). PI(3,4)P2 formation by PIK3C2A contributes to maturation of clathrin-coated pits by promoting the recruitment of BAR-domain containing proteins such as SNX9, which stimulate membrane curvature required for vesicle formation and eventual fission (Posor et al, 2013; reveiwed in Daumke et al, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O00443-1",
"P00533-1",
"P22681-1",
"Q2M2I8-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-8868071",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8868071"
}
]
},
{
"id": "R-HSA-8868072",
"name": "Clathrin-associated PIK3C2A phosphorylates PI(4)P to PI(3,4)P2",
"equation": "",
"summary": "Clathrin-associated PIK3C2A catalyzes the conversion of PI(4)P to PI(3,4)P2, which contributes to the recruitment of BAR domain proteins such as SNX9 to the clathrin-coated pit (Domin et al, 2000; Gaidarov et al, 2001; Gaidarov et al, 2005; Posor et al, 2013; reviewed in Daumke et al, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O00443-1",
"P00533-1",
"P22681-1",
"Q2M2I8-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-8868072",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8868072"
}
]
},
{
"id": "R-HSA-8868230",
"name": "SNX9 recruits components of the actin polymerizing machinery",
"equation": "",
"summary": "Actin polymerization is not absolutely required for clathrin-mediated endocytosis, and disruption of actin does not interfere with the early stages of clathrin-coated pit formation. Actin is required to complete vesicle formation under conditions of high membrane tension, such as on the apical side of polarized epithelial cell, while actin is dispensable for this process in the absence of membrane tension (Boulant et al, 2011). In cases where actin is required, it appears to be recruited late to the emerging clathrin-coated pit, just prior to or coincident with the recruitment of dynamin and vesicle scission (Taylor et al, 2011; Taylor et al, 2012; reviewed in McMahon and Boucrot, 2011). Recruitment of actin depends on the ARP2/3 complex, and cortactin or the neural Wiscott-Aldrich syndrome proteins WASL. These proteins, in turn, are recruited through interactions with N-BAR domain containing proteins such as SNX9 (Yarar et al, 2007; Shin et al, 2007; Shin et al, 2008; Ferguson et al, 2009; reviewed in Lundmark and Carlsson, 2009; McMahon and Boucrot, 2011).
HIP1 and HIP1R are additional components of the late clathrin-coated pit that interact with clathrin and AP-2 and may contribute to actin nucleation (Waelter et al, 2001; Mishra et al, 2001;Metzler et al, 2001; Legendre-Guillemin et al, 2002; Wilbur et al, 2008; Taylor et al, 2011).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P22681-1",
"P60709-1",
"Q2M2I8-1",
"P63261-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-8868230",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8868230"
}
]
},
{
"id": "R-HSA-8868236",
"name": "BAR domain proteins recruit dynamin",
"equation": "",
"summary": "Dynamin is a large GTPase whose GTP hydrolysis activity is required for the scission of clathrin-coated vesicles from the plasma membrane (reviewed in Ferguson and De Camilli, 2012). Dynamin is recruited to the plasma membrane through protein-protein interactions with many components of the clathrin-coated pit including ITSNs, SNX9 and 18 and amphiphysin (Lundmark and Carlsson, 2003; Soulet et al, 2005; David et al, 1996; Owen et al, 1998; Shupliakov et al, 1997). Although dynamin is recruited at lower levels throughout formation of the clathrin-coated pit, the bulk of dynamin is recruited at late stages, after the incorporation of BAR domain-containing proteins and actin-polymerizing factors (Ferguson et al, 2009; Taylor et al, 2011; Taylor et al, 2012; Posor et al, 2013; Meineke et al, 2013; Aguet et al, 2013; reviewed in Daumke et al, 2014). Several BAR domain proteins have SH3 domains that bind the proline rich domain (PRD) of dynamin. These interactions regulate dynamin GTPsae activity and vesicle formation (Neuman and Schmid, 2013). To facilitate scission of a clathrin-coated pit from the plasma membrane, dynamin self assembles into helical oligomers, stimulating its GTPase activity and contributing to the membrane remodeling required to form the neck of the emerging vesicle (Sweitzer and Hinshaw 1998; Yoshida et al, 2004; Chappie et al, 2010; Faelber et al, 2011; Ford et al, 2011; reviewed in McMahon and Boucrot, 2011; Daumke et al, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05193-1",
"Q9UQ16-1",
"P00533-1",
"P22681-1",
"P60709-1",
"Q2M2I8-1",
"P50570-1",
"P63261-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-8868236",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8868236"
}
]
},
{
"id": "R-HSA-8868648",
"name": "SYNJ hydrolyze PI(4,5)P2 to PI(4)P",
"equation": "",
"summary": "Inositol-5-phosphatases like SYNJs and OCRL hydrolyze PI(4,5)P2 to PI(4)P. In the context of CME, this promotes the abortive turnover (disassembly) of some CCPs, contributes to the dynamin-mediated scission of the clathrin-coated vesicle neck, and promotes clathrin uncoating following scission (Guan et al, 2010; Cremona et al, 1999; Mani et al, 2007; Chang-Ileto et al, 2011; Antonescu et al, 2011; reviewed in McMahon and Boucrot, 2011; Daumke et al, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05193-1",
"Q9UQ16-1",
"P00533-1",
"P22681-1",
"P60709-1",
"Q2M2I8-1",
"P50570-1",
"P63261-1",
"Q01968-1",
"O15056-1",
"P13569-1",
"O43426-1"
],
"evidence": [
{
"id": "R-HSA-8868648",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8868648"
}
]
},
{
"id": "R-HSA-8868651",
"name": "Endophilins recruit synaptojanins to the clathrin-coated pit",
"equation": "",
"summary": "Synaptojanin (SYNJ) 1 and 2 are inositol-5-phosphatases that sequentially convert PI(4,5)P2 to PI(4)P and PI (Cremona et al 1999; reviewed in Billcliff and Lowe, 2014). Conversion of PI(4,5)P2 to PI(4)P and PI accompanies maturation of the clathrin-coated pit, and consistent with this, SYNJ proteins are recruited to the clathrin-coated pit through interactions with a number of endocytic proteins including ITSNs, EPS15, PACSIN proteins and endophilins, as well as with clathrin and AP-2 (Haffner et al, 1997; Cestra et al, 1999; Maire et al, 2004; Schuske et al, 2003; Verstreken et al, 2003; Modregger et al, 2000; Perera et al 2006; Milosevic et al, 2011; reviewed in Dittman and Ryan, 2009). SYJN1 exists in two isoforms, a longer 170 kDA isoform and a shorter 145 kDA isoform, with slightly different roles. The recruitment and activity of SYNJ1-145 appears to largely coincide with that of dynamin at later stages of vesicle formation, while the SYNJ1-170 isoform also plays earlier roles in stabilizing the growing clathrin-coated vesicle (Perera et al, 2006; Taylor et al, 2011; Antonescu et al, 2011). SYNJ-mediated hydrolysis of PI(4,5)P2 to PI(4)P is most efficient on highly curved, endophilin-coated tubules of the vesicle neck and contributes to dynamin-mediated membrane scission (Chang-Ileto et al, 2011; reviewed in Daumke et al, 2014; McMahon and Boucrot, 2011).
In addition to SYNJ1 and 2, other inositol-5-phosphatases are also recruited to the CCP at the time of scission. These include OCRL, which is recruited through interaction with clathrin as well as the RAB5 interactor APPL1 (Erdmann et al, 2007; Mao et al, 2009; Taylor et al, 2011; Nandez et al, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05193-1",
"Q9UQ16-1",
"P00533-1",
"P22681-1",
"P60709-1",
"Q2M2I8-1",
"P50570-1",
"P63261-1",
"Q01968-1",
"O15056-1",
"P13569-1",
"O43426-1"
],
"evidence": [
{
"id": "R-HSA-8868651",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8868651"
}
]
},
{
"id": "R-HSA-8868658",
"name": "HSPA8-mediated ATP hydrolysis promotes vesicle uncoating",
"equation": "",
"summary": "HSPA8 hydrolyzes ATP to promote dissociation of the clathrin coat from the vesicle (reviewed in Sousa and Lafer, 2015). Interaction of HSPA8 with the C-terminal tail of clathrin may sterically block re-stabilization of the clathrin coat, which is thought to undergo transient cycles of 'breathing', or loosening of the interactions between the triskelions (Barouch et al, 1997; Rapoport et al, 2008; Xing et al, 2010). Alternately, HSPA8 may destabilize the clathrin coat through intermolecular collisions with the coat (reveiwed in Sousa and Lafer, 2015). The HSPA8-clathrin interaction persists once clathrin has been removed from the vesicle. This is thought to preclude aberrant repolymerization of clathrin by sequestering free clathrin (Schlossman et al, 1984; reviewed in Sousa and Lafer, 2015).",
"cellular_location": "clathrin-coated endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05193-1",
"Q9UQ16-1",
"P00533-1",
"P22681-1",
"P60709-1",
"Q2M2I8-1",
"P11142-1",
"P50570-1",
"P63261-1",
"O14976-1",
"Q01968-1",
"O15056-1",
"P13569-1",
"O75061-1",
"O43426-1"
],
"evidence": [
{
"id": "R-HSA-8868658",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8868658"
}
]
},
{
"id": "R-HSA-8868659",
"name": "Clathrin recruits auxilins to the clathrin-coated vesicle",
"equation": "",
"summary": "After fission from the plasma membrane, auxilin proteins DNAJC6 and GAK are recruited to the vesicle through interaction with clathrin and phosphoinositides, in particular PI4P (Greener et al, 2000; Lee et al, 2006; Massol et al, 2006; Taylor et al, 2011; Scheele et al, 2001; Fotin et al, 2004a; Fotin et al, 2004b; Guan et al, 2010; reviewed in McMahon and Boucrot, 2011; Sousa and Lafer, 2015). Auxilin in turn recruits the ATPase HSPA8 (also known as HSC70) , which uses the energy from ATP hydrolysis to remove the clathrin-coat from the vesicle, priming it for fusion with a subsequent endosomal compartment (Schlossman et al, 1984; Ungewickell et al, 1995; Rappoport et al, 2008; Xing et al, 2010; Bocking et al, 2011; Rothnie et al, 2011; reviewed in McMahon and Boucrot, 2011; Sousa and Lafer, 2015).",
"cellular_location": "clathrin-coated endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05193-1",
"Q9UQ16-1",
"P00533-1",
"P22681-1",
"P60709-1",
"Q2M2I8-1",
"P50570-1",
"P63261-1",
"O14976-1",
"Q01968-1",
"O15056-1",
"P13569-1",
"O75061-1",
"O43426-1"
],
"evidence": [
{
"id": "R-HSA-8868659",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8868659"
}
]
},
{
"id": "R-HSA-8868660",
"name": "Auxilin recruits HSPA8:ATP to the clathrin-coated vesicle",
"equation": "",
"summary": "HSPA8 (also known as HSC70) is recruited to the clathrin-coated vesicle through interaction with DNA J proteins GAK and DNAJC6 (Rapoport et al, 2008; Xing et al, 2010; reviewed in Sousa and Lafer, 2015). Recent studies examining the stoichiometry of uncoating predict between one and three HSPA8 molecules are required per clathrin triskelion for maximal uncoating in vitro (Bocking et al, 2011; Rothnie et al, 2011). After ATP hydrolysis, HSPA8 remains associated with the liberated clathrin, which prevents aberrant repolymerization and association of clathrin (Schlossman et al, 1984; reviewed in Sousa and Lafer, 2015).",
"cellular_location": "clathrin-coated endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05193-1",
"Q9UQ16-1",
"P00533-1",
"P22681-1",
"P60709-1",
"Q2M2I8-1",
"P11142-1",
"P50570-1",
"P63261-1",
"O14976-1",
"Q01968-1",
"O15056-1",
"P13569-1",
"O75061-1",
"O43426-1"
],
"evidence": [
{
"id": "R-HSA-8868660",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8868660"
}
]
},
{
"id": "R-HSA-8868661",
"name": "Dynamin-mediated GTP hydrolysis promotes vesicle scission",
"equation": "",
"summary": "Self-assembly of dynamin around the neck of the emerging clathrin-coated vesicle stimulates its GTPase activity. This in turn promotes a conformational change in dynamin organization that is required for membrane fission (Hinshaw and Schmid, 1995; Sweitzer and Hinshaw, 1998; Takei et al, 1999; Yoshida et al, 2004; Chappie et al, 2010; Chappie et al, 2011; Ford et al, 2011; Faelber et al, 2011; reviewed in Daumke et al, 2014).",
"cellular_location": "plasma membrane, clathrin-coated endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05193-1",
"Q9UQ16-1",
"P00533-1",
"P22681-1",
"P60709-1",
"Q2M2I8-1",
"P50570-1",
"P63261-1",
"Q01968-1",
"O15056-1",
"P13569-1",
"O43426-1"
],
"evidence": [
{
"id": "R-HSA-8868661",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8868661"
}
]
},
{
"id": "R-HSA-8869438",
"name": "Dissociation of clathrin-associated proteins",
"equation": "",
"summary": "After the removal of the clathrin coat, it is likely that many of the proteins that contributed to vesicle formation are lost, although the timing and mechanism of this step are poorly understood (reviewed in McMahon and Boucrot, 2011; Lemmon, 2001).",
"cellular_location": "clathrin-coated endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P51148-1",
"Q05193-1",
"Q9UQ16-1",
"P00533-1",
"P22681-1",
"P60709-1",
"P50570-1",
"P63261-1",
"P20339-1",
"O14976-1",
"Q01968-1",
"O15056-1",
"P61020-1",
"P13569-1",
"O75061-1",
"O43426-1"
],
"evidence": [
{
"id": "R-HSA-8869438",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8869438"
}
]
},
{
"id": "R-HSA-8871193",
"name": "Dissociation of AAK1 and dephosphorylation of AP-2 mu2",
"equation": "",
"summary": "GAPVD1 binds the alpha adaptin ear domain of AP-2 mu2, activating its RAB5-directed GEF activity and displacing AAK1. AAK1 displacement results in a net dephosphorylation of the AP-2 mu2 subunit, destabilizing the interaction of AP-2 with the vesicle membrane (Sato et al, 2005; Smerdjieva et al, 2008). In addition, RAB5 contributes to PI(4,5)P2 turnover through recruitment of a PI3K or PI phosphatase, and this also destabilizes the interaction of AP-2 with the membrane (Smerdjieva et al, 2008; Christoforidis et al, 1999; Shin et al, 2005).",
"cellular_location": "clathrin-coated endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P51148-1",
"Q05193-1",
"Q9UQ16-1",
"P00533-1",
"P22681-1",
"P60709-1",
"Q2M2I8-1",
"P50570-1",
"P63261-1",
"P20339-1",
"O14976-1",
"Q01968-1",
"O15056-1",
"P61020-1",
"P13569-1",
"O75061-1",
"O43426-1"
],
"evidence": [
{
"id": "R-HSA-8871193",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8871193"
}
]
},
{
"id": "R-HSA-8871194",
"name": "RAB5 and GAPVD1 bind AP-2",
"equation": "",
"summary": "RAB5 is a small GTPase that is implicated in clathrin-mediated endocytosis (Chavrier et al, 1990; McLauchlan et al, 1998; Shin et al, 2002; Taylor et al, 2011; reviewed in Stenmark, 2009; Wandiger-Ness and Zerial, 2014). Recent studies have shown that RAB5 and its associated GEF GAPVD1 may contribute to AP-2 uncoating by displacing AAK1 and promoting the net dephosphorylation of the AP-2 mu2 subunit. This is predicted to destabilize interactions with the plasma membrane and promote uncoating (Sato et al, 2005; Hunker et al, 2006; Smerdjieva et al, 2008). RAB5 and GAPVD1 also increase PI(4,5)P2 turnover, likely through recruitment of a class I PI3K or a PI phosphatase (Christoforidis et al, 1999; Shin et al, 2005).",
"cellular_location": "clathrin-coated endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P51148-1",
"Q05193-1",
"Q9UQ16-1",
"P00533-1",
"P22681-1",
"P60709-1",
"Q2M2I8-1",
"P50570-1",
"P63261-1",
"P20339-1",
"O14976-1",
"Q01968-1",
"O15056-1",
"P61020-1",
"P13569-1",
"O75061-1",
"O43426-1"
],
"evidence": [
{
"id": "R-HSA-8871194",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8871194"
}
]
},
{
"id": "R-HSA-8874797",
"name": "EGFR gene expression is stimulated by TFAP2C",
"equation": "",
"summary": "Binding of TFAP2C homodimers to the EGFR gene promoter region stimulates EGFR transcription and may play an important role in the etiology of luminal breast cancer (Park et al. 2015, de Andrade et al. 2016).",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-8874800"
],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-8874797",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8874797"
}
]
},
{
"id": "R-HSA-8951490",
"name": "CIN85 dissociates from EGF:p-6Y-EGFR:CBL:Beta-Pix:CDC42:GTP:CIN85",
"equation": "",
"summary": "High concentrations of active CDC42 (bound to GTP) and Beta-Pix may promote the binding of Beta-Pix to CBL, pushing out the usually preferred binding partner CIN85 (SH3KBP1) from the CBL complex. This competitive mechanism could block the CIN85-imposed clustering phenomenon on CBL that is required for tighter binding (Schmidt et al. 2006).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P22681-1",
"P60953-2"
],
"evidence": [
{
"id": "R-HSA-8951490",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8951490"
}
]
},
{
"id": "R-HSA-9018572",
"name": "EGFR phosphorylates NOTCH3",
"equation": "",
"summary": "EGFR phosphorylates intracellular domain of NOTCH3 (NICD3) on an unknown tyrosine residue. EGFR signaling inhibits NICD3-mediated transcription. It is not known whether EGFR-mediated phosphorylation of NICD3 affects NICD3 nuclear translocation or the formation of the NOTCH3 coactivator complex. Erlotinib treatment, which inhibits EGFR activation, results in increased NOTCH3 signaling and induction of stem-like phenotype in treated cells (Arasada et al. 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-9018581"
],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-9018572",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9018572"
}
]
},
{
"id": "R-HSA-9018573",
"name": "NOTCH3 binds activated EGFR",
"equation": "",
"summary": "The intracellular domain of NOTCH3 (NICD3) co-immunoprecipitates with ligand activated, autophosphorylated EGFR. Binding of NOTCH3 to EGFR is inhibited by erlotinib treatment, which prevents EGFR activation (Arasada et al. 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-9018573",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9018573"
}
]
},
{
"id": "R-HSA-9609689",
"name": "HCMV Binds to the Host Cell via heparan sulfate proteoglycans (HSPG)",
"equation": "",
"summary": "Viral attachment and penetration of Human Cytomegalovirus (HCMV) occurs either via direct HCMV fusion with the cell membrane or via endocytosis. The endocytic mechanism occurs with cell types including endothelial and epithelial cells, where the pentameric viral protein complex, gH:gL:p128:p130:p131A, facilitates entry.",
"cellular_location": "extracellular region",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-9609689",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9609689"
}
]
},
{
"id": "R-HSA-9610867",
"name": "HCMV Binds Host Cell Receptor - Endocytic Pathway",
"equation": "",
"summary": "Viral attachment and penetration of Human Cytomegalovirus (HCMV) occurs either via direct HCMV fusion with the cell membrane or via endocytosis. The endocytic mechanism occurs with cell types including endothelial and epithelial cells, where the pentameric viral protein complex, gH:gL:p128:p130:p131A, facilitates entry.",
"cellular_location": "extracellular region",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-9610867",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9610867"
}
]
},
{
"id": "R-HSA-9611147",
"name": "Endocytic Uptake of HCMV Virion",
"equation": "",
"summary": "Once the pentameric viral protein complex, gH:gL:p128:p130:p131A, facilitates attchment of the Human Cytomegalovirus (HCMV) endocytic uptake allows the virion to enter epithelial and endothelial cells. The virion is released from the endocytic vesicle by low-pH-dependent fusion of the virion coat with endosomes membrane.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-9611147",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9611147"
}
]
},
{
"id": "R-HSA-9611158",
"name": "Fusion of HCMV Envelope with Plasma Membrane",
"equation": "",
"summary": "Once Human cytomegalovirus (HCMV) initial attachs to cell surface heparan sulfate proteoglycans (HSPGs), the virus fuses with thecell membrane.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-9611158",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9611158"
}
]
},
{
"id": "R-HSA-9625465",
"name": "E2-mediated FOS gene expression",
"equation": "",
"summary": "The FOS gene encodes FOS, a leucine zipper protein that dimerizes with other FOS, JUN or ATF family members to form the ubiquitous transcription factor complex AP-1 (reviewed in Milde-Langosch, 2005; Hess et al, 2004). AP-1 transcription factors regulate gene expression in response to numerous upstream stimuli, including growth factors, hormones and cytokines and influence proliferation, differentiation and apoptosis, among other processes (reviewed in Shaulina et al, 2002; Thiel and Rossler, 2017).
Transcription of the FOS gene is regulated in part by binding of TCF (a complex of SRF and phosphorylated ELK1) to the serum response element (SRE) in the promoter (Marais et al, 1993; Gille et al, 1995; Duan et al, 2001; reviewed in Treisman, 1995)",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-8948462"
],
"output_participant_list": [
"R-HSA-450216"
],
"enzyme_list": [
"P00533-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-9625465",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9625465"
}
]
},
{
"id": "R-HSA-9625482",
"name": "PTK2 binds activated EGFR",
"equation": "",
"summary": "PTK2 (also known as FAK, focal adhesion kinase) binds to the activated EGFR receptor as assessed by affinity chromatography and co-immunoprecipitation (Sieg et al, 2000; Thelemann et al, 2005; Liu et al, 2010). Stimulation of the EGFR pathway increases PTK2 phosphorylation at Y397, and FAK phosphorylation contributes to cell migration and tumorigenicity (Tamura et al, 1998; Gu et al, 1999; Sieg et al, 2000; Liu et al, 2010; reviewed in Zhu et al, 2018). PTK2-stimulated cell motility depends on integrins and is transduced through phosphorylated MAPK3 and MAPK1 (also known as ERK1 and ERK2) (Sieg et al, 2000; Thelemann et al, 2000; Liu et al, 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-9625482",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9625482"
}
]
},
{
"id": "R-HSA-9625487",
"name": "PTK2 autophosphorylates downstream of EGFR",
"equation": "",
"summary": "Stimulation of cells with either E2 (beta-estradiol), tamoxifen or G1 (a GPER1 agonist) enhances EGFR-dependent FAK autophosphorylation at Y397 (Sieg et al, 2000; Liu et al, 2010; Tsai et al, 2013). Signaling occurs through both GPER1 and ER alpha (ESR1) and induces cell proliferation and migration through the EGFR-PI3K-ERK pathway (Liu et al, 2010; Tsai et al, 2013; reviewed in Zhu et al, 2018). FAK autophosphorylation is also required for FOS (c-fos) induction downstream of E2 (Liu et al, 2010; Tsai et al, 2013; Maggiolini et al, 2004; Vivacqua et al, 2006a,b).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-9625487",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9625487"
}
]
},
{
"id": "R-HSA-9634702",
"name": "LINC01139 promotes phosphorylation of HIF1A by LRRK2",
"equation": "",
"summary": "LRRK2 serine/threonine kinase, activated via long non-coding RNA LINC01139 (LINK-A) mediated recruitment to phosphorylated GPNMB (bound to HBEGF-activated EGFR), phosphorylates hypoxia inducible factor 1 alpha (HIF1A) at serine residue S797. LRRK2-mediated phosphorylation of HIF1A at S797 promotes association of HIF1A with EP300 (p300) transcriptional co-activator and inhibits association of HIF1A with a transactivation inhibitor HIF1AN (FIH) (Lin et al. 2016).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [
"R-HSA-8857584"
],
"output_participant_list": [
"R-HSA-9634700"
],
"enzyme_list": [
"Q13882-1",
"P00533-1",
"Q5S007-1"
],
"evidence": [
{
"id": "R-HSA-9634702",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9634702"
}
]
},
{
"id": "R-HSA-9664567",
"name": "ERBB2 KD mutants heterodimerize",
"equation": "",
"summary": "The following ERBB2 KD mutants were directly or indirectly shown to form heterodimers with EGFR:
ERBB2 L755P (Kancha et al. 2011 \u2013 indirect, higher catalytic activity in the presence of EGF stimulated EGFR);
ERBB2 L755S (Kancha et al. 2011, Bose et al. 2013 \u2013 indirect, higher kinase activity in the presence of EGFR);
ERBB2 I767M (Bose et al. 2013 \u2013 indirect, EGFR is phosphorylated in the presence of ERBB2 I767M);
ERBB2 D769H (Bose et al. 2013 \u2013 indirect, trans autophosphorylation in the presence of EGFR);
ERBB2 D769Y (Bose et al. 2013 \u2013 indirect, trans autophosphorylation in the presence of EGFR);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013 \u2013 indirect, increased catalytic activity in the presence of EGF activated EGFR);
ERBB2 G778_P780dup (Bose et al. 2013, Suzawa et al. 2016, Ogoshi et al. 2019 \u2013 indirect, trans-autophosphorylates in the presence of EGFR);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013 \u2013 indirect, trans-autophosphorylation in the presence of EGF-stimulated EGFR);
ERBB2 V842I (Bose et al. 2013 \u2013 indirect, trans-autophosphorylation in the presence of EGFR);
ERBB2 T862A (Kancha et al. 2011 \u2013indirect, increased catalytic activity in the presence of EGF activated EGFR);
ERBB2 H878Y (Kancha et al. 2011 \u2013 indirect, activated in the presence of EGF-stimulated EGFR);
ERBB2 R896C (Bose et al. 2013 \u2013 indirect, trans autophosphorylation in the presence of EGFR);
ERBB2 L755_T759del (Bose et al. 2013 \u2013 indirect, EGFR phosphorylated in the presence of the mutant);
ERBB2 Y772_A775dup (Wang et al. 2006 - direct)
The following ERBB2 KD mutants were directly or indirectly shown to form heterodimers with ERBB3:
ERBB2 L755P (Kancha et al. 2011 \u2013 indirect, higher catalytic activity in the presence of neuregulin stimulated ERBB3);
ERBB2 L755S (Croessmann et al. 2019 \u2013 direct, mutant forms heterodimers with ERBB3 at a higher rate than the wild type ERBB2; Kancha et al. 2011, Bose et al. 2013 \u2013 indirect, higher kinase activity in the presence of ERBB3);
ERBB2 I767M (Ng et al. 2015 \u2013 indirect, catalytic activity induced by neuregulin-1 (NRG1));
ERBB2 D769H (Collier al. 2013 \u2013 direct, 3-fold increase in catalytic activity upon heterodimerization);
ERBB2 D769Y (Collier al. 2013 \u2013 direct, 3-fold increase in catalytic activity upon heterodimerization);
ERBB2 G776S (Fan et al. 2008 \u2013 indirect, trans-autophosphorylation increased in the presence of the mutant);
ERBB2 V777L (Croessmann et al. 2019 \u2013 direct, mutant forms heterodimers with ERBB3 at a higher rate than the wild type ERBB2; Kancha et al. 2011, Bose et al. 2013 \u2013 indirect, increased catalytic activity in the presence of neuregulin-activated ERBB3);
ERBB2 T798M (Rexer et al. 2013 \u2013 direct, co-immunoprecipitates with ERBB3; Kancha et al. 2011, Rexer et al. 2013 \u2013 indirect, trans-autophosphorylation in the presence of neuregulin-stimulated ERBB3);
ERBB2 V842I (Bose et al. 2013 \u2013 indirect, trans-autophosphorylation in the presence of ERBB3);
ERBB2 T862A (Kancha et al. 2011 - indirect, increased catalytic activity in the presence of neuregulin-activated ERBB3);
ERBB2 L869R (Hanker et al. 2017 \u2013 direct, heterodimerization may be increased in the presence of ERBB3 E928G mutant);
ERBB2 H878Y (Kancha et al. 2011 \u2013 indirect, activated in the presence of neuregulin-stimulated ERBB3);
ERBB2 L755_T759del (Bose et al. 2013 \u2013 indirect, ERBB3 phosphorylated in the presence of the mutant);
ERBB2 Y772_A775dup (Wang et al. 2006 - direct)
Heterodimerizaton of ERBB2 KD mutants with ERBB4 has not been tested and ERBB4 is shown as a heterodimerization candidate.
Heterodimerization properties of the following ERBB2 KD mutants have not been tested and they are annotated as candidates based on their substituted residue being identical to the substituted residue of functionally studied mutants and based on computational prediction of the pathogenicity of the mutation in COSMIC database:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769N
ERBB2 V777E
ERBB2 V777M
ERBB2 T733I
ERBB2 T798I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9664567",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664567"
}
]
},
{
"id": "R-HSA-9664588",
"name": "ERBB2 KD mutants trans-autophosphorylate",
"equation": "",
"summary": "The following ERBB2 KD mutants were shown to undergo trans-autophosphorylation in the presence of EGFR:
ERBB2 L755P (Bose et al. 2013);
ERBB2 L755S (Kancha et al. 2011, Bose et al. 2013);
ERBB2 I767M (Bose et al. 2013);
ERBB2 D769H (Bose et al. 2013);
ERBB2 D769Y (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Bose et al. 2013, Suzawa et al. 2016, Ogoshi et al. 2019);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013)
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);ERBB2 Y772_A775dup (Wang et al. 2006)
The following ERBB2 KD mutants were shown to undergo trans-autophosphorylation in the presence of ERBB3:
ERBB2 L755P (Bose et al. 2013);
ERBB2 L755S (Kancha et al. 2011, Bose et al. 2013);
ERBB2 I767M (Ng et al. 2015 \u2013 indirect, in response to neuregulin-1 (NRG1) treatment);
ERBB2 D769H (Bose et al. 2013, Collier et al. 2013);
ERBB2 D769Y (Bose et al. 2013, Collier et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 G776S (Fan et al. 2008);
ERBB2 Y772_A775dup (Wang et al. 2006)
In the majority of studies, trans-autophosphorylation of specific tyrosine residues of ERBB2 KD mutants and its heterodimerization partners, EGFR and ERBB3 (and ERBB4), has not been examined, and they are assumed to be identical to tyrosine residues that undergo trans-autophosphorylation in the wild type ERBB2 heterodimers. ERBB2 H878Y is also phosphorylated on the substitution tyrosine Y878 (Hu, Wan et al. 2015). EGFR and ERBB3 undergo trans-autophosphorylation in the presence of ERBB2 L755_T759del mutant, while ERBB2 L755_T759del remains unphosphorylated (Bose et al. 2013).
Phosphorylation at tyrosine Y1221 was demonstrated for the following ERBB2 KD mutants:
ERBB2 L755S (Trowe et al. 2008);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 L869R (Hanker et al. 2017);
Phosphorylation at tyrosine Y1222 was demonstrated for the following ERBB2 KD mutants:
ERBB2 L755S (Trowe et al. 2008);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 L869R (Hanker et al. 2017);
Phosphorylation at tyrosine Y1248 was demonstrated for the following ERBB2 KD mutants:
ERBB2 L755S (Croessmann et al. 2019);
ERBB2 V777L (Croessmann et al. 2019);
ERBB2 T798M (Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 Y772_A775dup (Wang et al. 2006);
Phosphorylation of EGFR at tyrosine Y1068 was demonstrated in the presence of the following ERBB2 KD mutants:
ERBB2 T798M (Rexer et al. 2013);
ERBB2 Y772_A775dup (Wang et al. 2006)
Phosphorylation of ERBB3 at tyrosine Y1197 was demonstrated in the presence of the following ERBB2 KD mutants:
ERBB2 L755S (Croessmann et al. 2019);
ERBB2 V777L (Croessmann et al. 2019);
ERBB2 T798M (Rexer et al. 2013);
ERBB2 L869R (Hanker et al. 2017);
Phosphorylation of ERBB3 at tyrosine Y1289 was demonstrated in the presence of the following ERBB2 KD mutants:
ERBB2 Y772_A775dup (Wang et al. 2006, Minami et al. 2007);
Trans-autophosphorylation of the following ERBB2 KD mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9664588",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664588"
}
]
},
{
"id": "R-HSA-9664918",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:GAB1",
"equation": "",
"summary": "Many EGFR-binding ERBB2 KD mutants were shown to activate PI3K/AKT signaling, as evidenced by activating phosphorylation of AKT in the presence of these ERBB2 KD mutants. Phosphorylated heterodimers of the following ERBB2 KD mutants with EGFR are assumed to, like the wild type ERBB2:EGFR heterodimer, bind to the GRB2:GAB1 complex:
ERBB2 L755S (Kancha et al. 2011, Cocco et al. 2018, Croessmann et al. 2019);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015; heterodimerization with EGFR indirectly shown by Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of PI3K/AKT signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 H878R",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664918",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664918"
}
]
},
{
"id": "R-HSA-9664933",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K",
"equation": "",
"summary": "For the following EGFR-binding ERBB2 KD mutants that activate PI3K/AKT signaling, it is assumed that, like the wild type ERBB2:EGFR heterodimer, binding to the GRB2:GAB1 adaptor complex leads to recruitment of the PI3K complex:
ERBB2 L755S (Kancha et al. 2011, Cocco et al. 2018, Croessmann et al. 2019);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015; heterodimerization with EGFR indirectly shown by Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of PI3K/AKT signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 H878R",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664933",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664933"
}
]
},
{
"id": "R-HSA-9664940",
"name": "PI3K bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR converts PIP2 to PIP3",
"equation": "",
"summary": "For the following EGFR-binding ERBB2 KD mutants that were shown to activate PI3K/AKT signaling, it is assumed that heterodimers of these mutants with EGFR, like the wild type ERBB2:EGFR heterodimer, bind to the PI3K complex through GRB2:GAB1, leading to conversion of PIP2 to PIP3:
ERBB2 L755S (Kancha et al. 2011, Cocco et al. 2018, Croessmann et al. 2019);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015; heterodimerization with EGFR indirectly shown by Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of PI3K/AKT signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 H878R",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664940",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664940"
}
]
},
{
"id": "R-HSA-9664950",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants bind SHC1",
"equation": "",
"summary": "Many ERBB2 KD mutants were shown to activate RAS/RAF/MAPK signaling, evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). Based on downstream activation of RAS/RAF/MAPK cascade, it is assumed that phosphorylated heterodimers of the following ERBB2 KD mutants, like phosphorylated heterodimers of the wild type ERBB2, bind to SHC1:
ERBB2 L755P (Kancha et al. 2011);
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 I767M (Ng et al. 2015);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 G776S (Fan et al. 2008);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664950",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664950"
}
]
},
{
"id": "R-HSA-9664976",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants phosphorylate SHC1",
"equation": "",
"summary": "For the following ERBB2 KD mutants that were shown to activate RAS/RAF/MAPK signaling, it is assumed that they, like phosphorylated heterodimers of the wild type ERBB2, bind to SHC1 and phosphorylate it:
ERBB2 L755P (Kancha et al. 2011);
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 I767M (Ng et al. 2015);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 G776S (Fan et al. 2008);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664976",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664976"
}
]
},
{
"id": "R-HSA-9664983",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants recruit GRB2:SOS1 through SHC1",
"equation": "",
"summary": "For the following ERBB2 KD mutants that were shown to activate RAS/RAF/MAPK signaling, it is assumed that they, like phosphorylated heterodimers of the wild type ERBB2, bind to and phosphorylate SHC1, leading to recruitment of the GRB2:SOS1 complex:
ERBB2 L755P (Kancha et al. 2011);
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 I767M (Ng et al. 2015);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 G776S (Fan et al. 2008);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664983",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664983"
}
]
},
{
"id": "R-HSA-9664991",
"name": "RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants",
"equation": "",
"summary": "For the following ERBB2 KD mutants that were shown to activate RAS/RAF/MAPK signaling, it is assumed that they, like phosphorylated heterodimers of the wild type ERBB2, bind to and phosphorylate SHC1, leading to recruitment of the GRB2:SOS1 complex and activating guanyl-nucleotide exchange on RAS:
ERBB2 L755P (Kancha et al. 2011);
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 I767M (Ng et al. 2015);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 G776S (Fan et al. 2008);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9664991",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664991"
}
]
},
{
"id": "R-HSA-9665000",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:SOS1",
"equation": "",
"summary": "The following EGFR-binding ERBB2 KD mutants that were shown to activate RAS/RAF/MAPK signaling, evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3), are assumed to, like the wild type ERBB2:EGFR heterodimer, directly bind to the GRB2:SOS1 complex:
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015; binding to EGFR indirectly demonstrated by Bose et al. 2013);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 H878R
ERBB2 R896H",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665000",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665000"
}
]
},
{
"id": "R-HSA-9665009",
"name": "RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR",
"equation": "",
"summary": "The following EGFR-binding ERBB2 KD mutants that were shown to activate RAS/RAF/MAPK signaling, evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3), are assumed to, like the wild type ERBB2:EGFR heterodimer, directly bind to the GRB2:SOS1 complex, leading to activating guanyl nucleotide exchange on RAS:
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015; binding to EGFR indirectly demonstrated by Bose et al. 2013);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 H878R
ERBB2 R896H",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9665009",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665009"
}
]
},
{
"id": "R-HSA-9665032",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and EGFR phosphorylate PLCG1",
"equation": "",
"summary": "It is assumed that the following EGFR-binding ERBB2 mutants that were shown to activate PLCG1 (PLCgamma-1) signaling, evidenced by activating phosphorylation of PLCG1, recruit and phosphorylate PLCG1:
ERBB2 L755S (Bose et al. 2013);
ERBB2 I767M (Bose et al. 2013);
ERBB2 D769H (Bose et al. 2013);
ERBB2 D769Y (Bose et al. 2013);
ERBB2 V777L (Bose et al. 2013);
ERBB2 G778_P780dup (Bose et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 H878Y (Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
It is assumed that, like the wild type ERBB2:EGFR heterodimer, phosphorylated heterodimers of these ERBB2 KD mutants and EGFR recruit PLCG1.
ERBB2 L755_T759del does not activate PLCG1 signaling (Bose et al. 2013).
Activation of PLCG1 downstream of the following PLCG1 mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 V842E
ERBB2 H878R
ERBB2 R896H",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665032",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665032"
}
]
},
{
"id": "R-HSA-9665034",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind PLCG1",
"equation": "",
"summary": "Activating phosphorylation of PLCG1 (PLCgamma-1) is increased in the presence of the following EGFR-binding ERBB2 KD mutants:
ERBB2 L755S (Bose et al. 2013);
ERBB2 I767M (Bose et al. 2013);
ERBB2 D769H (Bose et al. 2013);
ERBB2 D769Y (Bose et al. 2013);
ERBB2 V777L (Bose et al. 2013);
ERBB2 G778_P780dup (Bose et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 H878Y (Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
It is assumed that, like the wild type ERBB2:EGFR heterodimer, phosphorylated heterodimers of these ERBB2 KD mutants and EGFR recruit PLCG1.
ERBB2 L755_T759del does not activate PLCG1 signaling (Bose et al. 2013).
Activation of PLCG1 downstream of the following PLCG1 mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 V842E
ERBB2 H878R
ERBB2 R896H",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665034",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665034"
}
]
},
{
"id": "R-HSA-9665388",
"name": "ERBB2 ECD mutants heterodimerize with EGFR",
"equation": "",
"summary": "ERBB2 extracellular domain (ECD) mutants harbor missense mutations that lead to substitutions of amino acid residues in the heterodimerization arm contact surface, involved in formation of ERBB2 heterodimers. The functionally studied ERBB2 ECD mutants, ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012) seem to preferntially heterodimerize with EGFR. Heterodimerization of ERBB2 G309E involves formation of disulfide bonds (Greulich et al. 2012).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665388",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665388"
}
]
},
{
"id": "R-HSA-9665389",
"name": "Heterodimers of ERBB2 ECD mutants and EGFR trans-autophosphorylate",
"equation": "",
"summary": "ERBB2 S310F shows stronger activation of downstream signaling than ERBB2 G309A and ERBB2 G309E, and is hyperphosphorylated on tyrosine residues in the C-tail (Greulich et al. 2012), while the C-tail phosphorylation of ERBB2 G309A (Bose et al. 2013) and ERBB2 G309E (Greulich et al. 2012) is comparable to the wild type ERBB2. Phosphorylation of EGFR was demonstrated in the presence of ERBB2 G309A (Bose et al. 2013). Except for ERBB2 C-tail tyrosine residues Y1221 and Y1222, which were shown to undergo trans-autophosphorylation in ERBB2 G309E, ERBB2 S310F and ERBB2 S310Y (Greulich et al. 2012), phosphorylation of specific tyrosine residues in ERBB2 and EGFR has not been examined and they are assumed to be the same as in the wild type ERBB2 heterodimers with EGFR.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665389",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665389"
}
]
},
{
"id": "R-HSA-9665404",
"name": "RAS guanyl nucleotide exchange mediated by the p-6Y- ERBB2 ECD mutants:EGF:p-6Y-EGFR:p-SHC1:GRB2:SOS1",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, can recruit the GRB2:SOS1 complex through phosphorylated SHC1, leading to guanyl nucleotide exchange on RAS and activation of RAS signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9665404",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665404"
}
]
},
{
"id": "R-HSA-9665406",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate SHC1",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, can bind to and phosphorylate SHC1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665406",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665406"
}
]
},
{
"id": "R-HSA-9665407",
"name": "PI3K bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR converts PIP2 to PIP3",
"equation": "",
"summary": "ERBB2 G309E and ERBB2 S310F activate PI3K/AKT signaling, demonstrated by activating phosphorylation of AKT1 (Greulich et al. 2012). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like the wild type heterodimers of ERBB2 and EGFR, can bind to the GRB2:GAB1 complex, leading to recruitment of the PI3K complex, which results in conversion of PIP2 to PIP3 and activation of the AKT signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665407",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665407"
}
]
},
{
"id": "R-HSA-9665408",
"name": "RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR through GRB2",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, can directly recruit the GRB2:SOS1 complex, leading to guanyl nucleotide exchange on RAS and activation of RAS signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9665408",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665408"
}
]
},
{
"id": "R-HSA-9665409",
"name": "GRB2:SOS1 binds to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, can directly recruit the GRB2:SOS1 complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665409",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665409"
}
]
},
{
"id": "R-HSA-9665410",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind PLCG1",
"equation": "",
"summary": "PLCgamma1 signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of PLCG1. It is assumed that heterodimers of ERBB2 ECD mutants and EGFR, like the wild type heterodimers of ERBB2 and EGFR, bind to PLCG1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665410",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665410"
}
]
},
{
"id": "R-HSA-9665411",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate PLCG1",
"equation": "",
"summary": "PLCgamma1 signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of PLCG1. It is assumed that heterodimers of ERBB2 ECD mutants and EGFR, like the wild type heterodimers of ERBB2 and EGFR, bind to and phosphorylated PLCG1, leading to activation of PLCG1 signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665411",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665411"
}
]
},
{
"id": "R-HSA-9665413",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR recruit GRB2:SOS1 through SHC1",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, can recruit the GRB2:SOS1 complex through phosphorylated SHC1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665413",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665413"
}
]
},
{
"id": "R-HSA-9665415",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K",
"equation": "",
"summary": "ERBB2 G309E and ERBB2 S310F activate PI3K/AKT signaling, demonstrated by activating phosphorylation of AKT1 (Greulich et al. 2012). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like the wild type heterodimers of ERBB2 and EGFR, can bind to the GRB2:GAB1 complex, leading to the recruitment of the PI3K complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665415",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665415"
}
]
},
{
"id": "R-HSA-9665416",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind SHC1",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, bind to SHC1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665416",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665416"
}
]
},
{
"id": "R-HSA-9665417",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind GRB2:GAB1",
"equation": "",
"summary": "ERBB2 G309E and ERBB2 S310F activate PI3K/AKT signaling, demonstrated by activating phosphorylation of AKT1 (Greulich et al. 2012). Activation of PI3K/AKT signaling downstream of ERBB2 G309A has not been tested. It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like the wild type heterodimers of ERBB2 and EGFR, can bind to the GRB2:GAB1 complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665417",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665417"
}
]
},
{
"id": "R-HSA-9665697",
"name": "ERBB2 TMD/JMD mutants hetrodimerize",
"equation": "",
"summary": "TMD/JMD mutants that are activating in the presence of wild type ERBB2, such as ERBB2 R678Q, may form homodimers with the wild type ERBB2 (Pahuja et al. 2018).
Based on trans-autophosphorylation of ERBB2 and its dimerization partners EGFR and ERBB3, the following ERBB2 TMD/JMD mutants are assumed to form heterodimers with EGFR and ERBB3:
ERBB2 S653C (de Martino et al. 2014)
ERBB2 R678Q (Bose et al. 2013, Pahuja et al. 2018).
TMD/JMD mutants that are activating in the presence of wild type ERBB2, such as ERBB2 R678Q, may form homodimers with the wild type ERBB2 (Pahuja et al. 2018).
Signaling by ERBB2 V659E, ERBB2 V659K, ERBB2 G660D, ERBB2 G660R, ERBB2 R677L, ERBB2 E693K and ERBB2 Q709L has not been sufficiently studied and they are annotated as candidates.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665697",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665697"
}
]
},
{
"id": "R-HSA-9665698",
"name": "Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind GRB2:SOS1",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3). It is assumed that heterodimers of ERBB2 TMD/JMD mutants and EGFR, like the wild type ERBB2:EGFR heterodimers, directly bind to GRB:SOS1 complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665698",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665698"
}
]
},
{
"id": "R-HSA-9665699",
"name": "Phosphorylated heterodimers of ERBB2 TMD/JMD mutants recruit GRB2:SOS1 through SHC1",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3) and SHC1. It is assumed that heterodimers of ERBB2 TMD/JMD mutants, like the wild type ERBB2 heterodimers, bind to and phosphorylate SHC1, leading to the recruitment of the GRB2:SOS1 complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665699",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665699"
}
]
},
{
"id": "R-HSA-9665700",
"name": "RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3) and SHC1. It is assumed that heterodimers of ERBB2 TMD/JMD mutants, like the wild type ERBB2 heterodimers, bind to and phosphorylate SHC1, leading to the recruitment of the GRB2:SOS1 complex and activation of RAS through guanyl nucleotide exchange.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9665700",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665700"
}
]
},
{
"id": "R-HSA-9665701",
"name": "Phosphorylated ERBB2 TMD/JMD heterodimers bind SHC1",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3) and SHC1. It is assumed that heterodimers of ERBB2 TMD/JMD mutants, like the wild type ERBB2 heterodimers, bind SHC1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665701",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665701"
}
]
},
{
"id": "R-HSA-9665704",
"name": "Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR phosphorylate PLCG1",
"equation": "",
"summary": "Activation of downstream PLCG1 signaling was demonstrated for ERBB2 R678Q, through activating tyrosine phosphorylation on PLCG1 (Bose et al. 2013). It is assumed that the heterodimer of ERBB2 R678Q and EGFR, like the wild type ERBB2:EGFR heterodimer, binds to and phosphorylates PLCG1, leading to activation of PLCgamma1 signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665704",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665704"
}
]
},
{
"id": "R-HSA-9665705",
"name": "Phosphorylated heterodimers of ERBB2 TMD/JMD mutants phosphorylate SHC1",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3) and SHC1. It is assumed that heterodimers of ERBB2 TMD/JMD mutants, like the wild type ERBB2 heterodimers, bind to and phosphorylate SHC1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665705",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665705"
}
]
},
{
"id": "R-HSA-9665706",
"name": "Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind PLCG1",
"equation": "",
"summary": "Activation of downstream PLCG1 signaling was demonstrated for ERBB2 R678Q, through activating tyrosine phosphorylation on PLCG1 (Bose et al. 2013). It is assumed that the heterodimer of ERBB2 R678Q and EGFR, like the wild type ERBB2:EGFR heterodimer, binds PLCG1.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665706",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665706"
}
]
},
{
"id": "R-HSA-9665707",
"name": "RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3). It is assumed that heterodimers of ERBB2 TMD/JMD mutants and EGFR, like the wild type ERBB2:EGFR heterodimers, directly bind to GRB:SOS1 complex, resulting in activation of RAS signaling to guanyl nucleotide exchange on RAS.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9665707",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665707"
}
]
},
{
"id": "R-HSA-9665709",
"name": "ERBB2 TMD/JMD heterodimers trans-autophosphorylate",
"equation": "",
"summary": "Phosphorylation of tyrosine residues in the C-tail of ERBB2 was shown for the following ERBB2 TMD/JMD mutants:
ERBB2 V659E (Pahuja et al. 2018);
ERBB2 V659K (Pahuja et al. 2018);
ERBB2 G660D (Pahuja et al. 2018);
ERBB2 G660R (Pahuja et al. 2018);
ERBB2 S653C (de Martino et al. 2014 - phosphorylation at Y1248 demonstrated);
ERBB2 R677L (Pahuja et al. 2018);
ERBB2 R678Q (Bose et al. 2013; de Martino et al. 2014 - phosphorylation at Y1248 demonstrated; Pahuja et al. 2018); ERBB2 Q709L (Pahuja et al. 2018)
Phosphorylation of tyrosine residues in the C-tail of EGFR was demonstrated for ERBB2 S653C (de Martino et al. 2014 - phosphorylation at Y1068) and ERBB2 R678Q (Bose et al. 2013; de Martino et al. 2014 - phosphorylation at Y1068).
Phosphorylation of tyrosine residues in the C-tail of ERBB3 was demonstrated for ERBB2 S653C (de Martino et al. 2014 - phosphorylation at Y1197) and ERBB2 R678Q (Bose et al. 2013; de Martino et al. 2014 - phosphorylation at Y1197).
Signaling by ERBB2 V659K, ERBB2 G660D, ERBB2 G660R, ERBB2 R677L, ERBB2 E693K and ERBB2 Q709L has not been sufficiently studied and they are annotated as candidates.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665709",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665709"
}
]
},
{
"id": "R-HSA-9674531",
"name": "AAMP binds EGFR",
"equation": "",
"summary": "AAMP (Angio-associated migratory cell protein) binds to EGFR. The interaction involves the intracellular domain of EGFR. AAMP binding, through an unknown mechanism, promotes EGFR dimerization, trans-autophosphorylation and downstream signaling, leading to activation of ERKs (MAPK1 and MAPK3) and expression of cyclin D1 (CCND1). Downregulation of AAMP inhibits proliferation of a non-small cell lung cancer (NSCLC) cell line and increases its sensitivity to EGFR-targeted chemotherapeutic drugs, and it also inhibits tumorigenesis in a mouse model (Yao et al. 2019).
In addition to lung cancer, AAMP overexpression is linked with poor prognosis in breast cancer, where AAMP level positively correlates with tumor grade. AAMP is overexpressed in breast ductal carcinoma in situ (DCIS) with necrosis (Adeyinka et al. 2002).",
"cellular_location": "cytoplasm, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-9674531",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674531"
}
]
},
{
"id": "R-HSA-9837625",
"name": "hRSV A enters host cell through macropinocytosis",
"equation": "",
"summary": "The study of human respiratory syncytial virus (RSV) A entry into HeLa and A549 cells using fluorescence microscopy and quantitative FACS assays has shown that, after attachment, RSV rapidly enters host cells by an actin-dependent process with characteristics of macropinocytosis. Findings are similar when primary bronchial epithelial cells are used (Krzyzaniak et al. 2013). Macropinocytosis requires activation of receptor tyrosine kinases (RTKs). The only RTK activated in experiments with HeLa and A549 cells is EGFR, and EGFR inhibitors block RSV entry (Krzyzaniak et al. 2013). EGFR has been reported to interact with the F protein of some RSV strains (Currier et al. 2016). However, in the airway epithelium, EGFR is mainly expressed in basal cells while the RTK IGF1R has been shown to be the binding partner for the F protein in the hRSV A2 strain and is required for RSV entry into ciliated epithelial cells of the airways (Griffiths et al. 2020). Protein kinase C signaling appears to be important for macropinocytosis-mediated entry of RSV (Krzyzaniak et al. 2013). Protein kinase C zeta (PRKCZ) has been shown to be activated downstream of IGF1R and seems to be important for RSV entry as it increases the concentration of the F protein binding partner, NCL, at the surface of ciliated airway epithelium (Griffiths et al. 2020). NCL has been reported to be involved in promotion of macropinocytosis (Reyes-Reyes et al. 2010; Reyes-Reyes et al. 2015). Other host cell factors implicated in RSV macropinocytosis are PI3K, RAC1 and CDC42 GTPases, PAK1 kinase - downstream effector of RAC1 and CDC42, myosin II - PAK1 target, Na+/H+ exchangers, and RAB5 macropinosome marker (Krzyzaniak et al. 2013).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P51148-1",
"P00533-1",
"P20339-1",
"P08069-1",
"P61020-1"
],
"evidence": [
{
"id": "R-HSA-9837625",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9837625"
}
]
},
{
"id": "R-HSA-9851407",
"name": "FAM83B, (FAM83A, FAM83D) bind EGFR",
"equation": "",
"summary": "Both recombinant and endogenous EGFR and FAM83B form a complex. The lysine residue K230 of FAM83B, conserved in other FAM83 family members, including FAM83A and FAM83D, is needed for binding to EGFR and stimulation of EGFR signaling. Through a mechanism that has not been elucidated, FAM83B stimulates basal and EGF-induced EGFR trans-autophosphorylation but dissociates from autophosphorylated EGFR (Cipriano et al. 2014).
FAM83B overexpression stimulates activation of MAPK and mTOR signaling downstream of EGFR, and prolongs activating EGFR, AKT and MAPK phosphorylation, increasing resistance to EGFR-targeting tyrosine kinase inhibitors (TKIs) AG1478, erlotinib, and CL387785 (Cipriano et al. 2012).
FAM83A overexpression similarly increases resistance of EGFR to EGFR-targeting TKIs AG1478, lapatinib, and gefitinib. In EGF-treated cells, tyrosine phosphorylation of FAM83A is increased, plausibly directly by EGFR, but the physical interaction between FAM83A and EGFR has not been reported. Downstream of EGFR activation, FAM83A associates with CRAF and PIK3R1. EGF treatment is not needed for FAM83A to interact with CRAF and PIK3R1 when FAM83A is overexpressed (Lee et al. 2012).
FAM83A-AS1 lncRNA, which is known to increase FAM83A expression, positively regulates EGFR signaling (Zhao et al. 2022).
FAM83D is highly expressed in invasive epithelial ovarian cancer. FAM83D-overexpressing cells demonstrate increased tyrosine phosphorylation of EGFR, as well as increased activating phosphorylation of downstream effectors of EGFR such as CRAF, ERK1/2 (MAPK3/1), and AKT (Zhang et al. 2019), but the direct interaction of FAM83D and EGFR has not been reported.
FAM83A and FAM83D are annotated as candidate binding partners or EGFR.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1"
],
"evidence": [
{
"id": "R-HSA-9851407",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9851407"
}
]
},
{
"id": "R-NUL-1248744",
"name": "Shc1 binds phosphorylated ERBB2:EGFR heterodimers",
"equation": "",
"summary": "Shc1 binds phosphorylated ERBB2:EGFR heterodimers in engineered mouse 32D cells (Pinkas-Kramarski et al. 1996).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-NUL-1248744",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-NUL-1248744"
}
]
},
{
"id": "R-NUL-1251923",
"name": "Plcg1 binds P-ERBB2:P-EGFR",
"equation": "",
"summary": "Mouse phospholipase C gamma 1 is phosphorylated by human recombinant ERBB2 exogenously expressed in mouse fibroblasts.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-NUL-1251923",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-NUL-1251923"
}
]
},
{
"id": "R-NUL-1251929",
"name": "Plcg1 phosphorylation by P-ERBB2:P-EGFR",
"equation": "",
"summary": "Mouse phospholipase C gamma 1 is phosphorylated by human recombinant ERBB2 exogenously expressed in mouse fibroblasts.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-NUL-1251929",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-NUL-1251929"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-HSA-167679",
"participant_name": "p-4Y-PLCG1 [plasma membrane]",
"crossref": [
{
"id": "P19174",
"database": "PRO",
"url": ""
},
{
"id": "PLCG1_HUMAN",
"database": "ZINC - Predictions - Purchasable",
"url": ""
},
{
"id": "NP_002651.2",
"database": "RefSeq",
"url": ""
},
{
"id": "2HSP",
"database": "PDB",
"url": ""
},
{
"id": "ENSP00000508698",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000124181",
"database": "OpenTargets",
"url": ""
},
{
"id": "1HSQ",
"database": "PDB",
"url": ""
},
{
"id": "PLCG1_HUMAN",
"database": "ZINC - Substances",
"url": ""
},
{
"id": "ENST00000373271",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000124181-PLCG1",
"database": "HPA",
"url": ""
},
{
"id": "ENST00000244007",
"database": "Ensembl",
"url": ""
},
{
"id": "P19174",
"database": "ZINC target",
"url": ""
},
{
"id": "P19174",
"database": "UniProt",
"url": ""
},
{
"id": "4FBN",
"database": "PDB",
"url": ""
},
{
"id": "ENSG00000124181",
"database": "Ensembl",
"url": ""
},
{
"id": "P19174",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "ENSP00000362368",
"database": "Ensembl",
"url": ""
},
{
"id": "4EY0",
"database": "PDB",
"url": ""
},
{
"id": "7NXE",
"database": "PDB",
"url": ""
},
{
"id": "P19174",
"database": "GeneCards",
"url": ""
},
{
"id": "1407",
"database": "Guide to Pharmacology - Targets",
"url": ""
},
{
"id": "ENSP00000244007",
"database": "Ensembl",
"url": ""
},
{
"id": "NP_877963.1",
"database": "RefSeq",
"url": ""
},
{
"id": "HMDBP00244",
"database": "HMDB Protein",
"url": ""
},
{
"id": "ENST00000685551",
"database": "Ensembl",
"url": ""
}
]
},
{
"participant_id": "R-HSA-179837",
"participant_name": "EGFR [plasma membrane]",
"crossref": [
{
"id": "P00533",
"database": "UniProt",
"url": ""
},
{
"id": "4RJ6",
"database": "PDB",
"url": ""
},
{
"id": "2ITP",
"database": "PDB",
"url": ""
},
{
"id": "4RJ7",
"database": "PDB",
"url": ""
},
{
"id": "2ITQ",
"database": "PDB",
"url": ""
},
{
"id": "6LUD",
"database": "PDB",
"url": ""
},
{
"id": "4RJ5",
"database": "PDB",
"url": ""
},
{
"id": "2ITO",
"database": "PDB",
"url": ""
},
{
"id": "6LUB",
"database": "PDB",
"url": ""
},
{
"id": "4RJ4",
"database": "PDB",
"url": ""
},
{
"id": "2ITN",
"database": "PDB",
"url": ""
},
{
"id": "4TKS",
"database": "PDB",
"url": ""
},
{
"id": "2ITV",
"database": "PDB",
"url": ""
},
{
"id": "4RJ8",
"database": "PDB",
"url": ""
},
{
"id": "2ITU",
"database": "PDB",
"url": ""
},
{
"id": "6P1D",
"database": "PDB",
"url": ""
},
{
"id": "6P1L",
"database": "PDB",
"url": ""
},
{
"id": "EGFR_HUMAN",
"database": "ZINC - Predictions - Purchasable",
"url": ""
},
{
"id": "2ITT",
"database": "PDB",
"url": ""
},
{
"id": "6S8A",
"database": "PDB",
"url": ""
},
{
"id": "6S9B",
"database": "PDB",
"url": ""
},
{
"id": "2ITX",
"database": "PDB",
"url": ""
},
{
"id": "4UIP",
"database": "PDB",
"url": ""
},
{
"id": "4UV7",
"database": "PDB",
"url": ""
},
{
"id": "2ITW",
"database": "PDB",
"url": ""
},
{
"id": "6P8Q",
"database": "PDB",
"url": ""
},
{
"id": "6S89",
"database": "PDB",
"url": ""
},
{
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{
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}
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}
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}
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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