MUC20 negatively regulates binding of GRB2-1 to MET (Higuchi et al. 2004).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851804",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851804"
}
]
},
{
"id": "R-HSA-8851827",
"name": "RAS guanyl nucleotide exchange by MET-bound GRB2:SOS1",
"equation": "",
"summary": "GRB2-1 is an adaptor protein for the RAS guanyl nucleotide exchange factor SOS1. GRB2-1, through association with activated receptor tyrosine kinases, such as MET, mediates recruitment of SOS1 to the plasma membrane. At the plasma membrane, SOS1 catalyzes guanyl nucleotide exchange on RAS proteins from GDP to GTP, resulting in RAS activation downstream of MET (Shen and Novak 1997, Besser et al. 1997).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P01112-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851827",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851827"
}
]
},
{
"id": "R-HSA-8851842",
"name": "MUC20 binds MET and inhibits GRB2 binding",
"equation": "",
"summary": "MUC20 (mucin 20) binds to both unphosphorylated and phosphorylated MET. MUC20 does not interfere with MET ligand-binding, dimerization and autophosphorylation, but association of MUC20 with activated MET specifically interferes with GRB2-1 recruitment to MET and the consequent RAS signaling activation. MUC20 oligomerization may facilitate binding to MET (Higuchi et al. 2004).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851842",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851842"
}
]
},
{
"id": "R-HSA-8851859",
"name": "Activated MET binds RANBP9 and SOS1",
"equation": "",
"summary": "RANBP9 binds to activated MET receptor and recruits RAS guanyl nucleotide exchange factor SOS1. RANBP9 can associate with unphosphorylated MET, but has a higher affinity for the activated receptor. The interaction involves the sprouty (SPRY) domain of RANBP9 and the tyrosine kinase domain of MET (Wang et al. 2002). RANBP9 competes with RANBP10 for MET binding. RANBP10 does not interact with SOS1, and RANBP10 binding inhibits activation of RAS downstream of MET (Wang et al. 2004).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851859",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851859"
}
]
},
{
"id": "R-HSA-8851866",
"name": "MET binds RANBP10",
"equation": "",
"summary": "The sprouty (SPRY) domain of RANBP10 binds the tyrosine kinase domain of MET. RANBP10 binding inhibits binding of RANBP9 to MET and, as RANBP10 does not interact with SOS1, RANBP10 binding interferes with RAS activation (Wang et al. 2004).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851866",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851866"
}
]
},
{
"id": "R-HSA-8851877",
"name": "RAS guanyl nucleotide exchange by SOS1 associated with RANBP9 and MET",
"equation": "",
"summary": "RAS guanyl nucleotide exchange factor SOS1 recruited to MET receptor through association with RANBP9 catalyzes guanyl nucleotide exchange on RAS from GDP to GTP, resulting in RAS activation (Wang et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P01112-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851877",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851877"
}
]
},
{
"id": "R-HSA-8851888",
"name": "MET binds SHC1-2",
"equation": "",
"summary": "Phosphorylated tyrosine residues Y1349 and Y1356 in the cytoplasmic tail of MET create docking sites for the SH2 domain of SHC1 splicing isoform 2 (SHC1-2) (Pelicci et al. 1995).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851888",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851888"
}
]
},
{
"id": "R-HSA-8851890",
"name": "MET phosphorylates SHC1-2",
"equation": "",
"summary": "Activated MET receptor phosphorylates the splicing isoform 2 of the adapter protein SHC1 (SHC1-2) on tyrosine residue Y317 (Pelicci et al. 1995).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851890",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851890"
}
]
},
{
"id": "R-HSA-8851899",
"name": "RAS guanyl nucleotide exchange by SOS1 bound to GRB2, SCH1-2 and MET",
"equation": "",
"summary": "SOS1, recruited to activated MET receptor via interaction of GRB2 with phosphorylated SHC1-2, catalyzes guanyl nucleotide exchange on RAS from GDP to GTP, resulting in RAS activation (Pelicci et al. 1995).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P01112-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851899",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851899"
}
]
},
{
"id": "R-HSA-8851900",
"name": "SHC1-2 bound to MET recruits GRB2:SOS1",
"equation": "",
"summary": "SHC1 splicing isoform 2 (SHC1-2) phosphorylated by MET on tyrosine residue Y317 recruits the GRB2:SOS1 complex to the activated MET receptor (Pelicci et al. 1995).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851900",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851900"
}
]
},
{
"id": "R-HSA-8851908",
"name": "Activated MET binds GAB1",
"equation": "",
"summary": "The adapter protein GAB1 can directly bind to phosphorylated MET receptor via its MET binding domain (MBD) (Schaeper et al. 2000, Lock et al. 2003).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851908",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851908"
}
]
},
{
"id": "R-HSA-8851919",
"name": "Activated MET binds GAB1 and GRB2",
"equation": "",
"summary": "While GAB1 can bind activated MET receptor directly, the presence of GRB2 results in a more stable association between GAB1 and MET (Weidner et al. 1996, Schaeper et al. 2000, Lock et al. 2003).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851919",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851919"
}
]
},
{
"id": "R-HSA-8851933",
"name": "MET phosphorylates GAB1",
"equation": "",
"summary": "Activated MET phosphorylates GAB1 on at least five tyrosine residues: Y447, Y472, Y589, Y627 and Y659 (Schaeper et al. 2000, Chan et al. 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851933",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851933"
}
]
},
{
"id": "R-HSA-8851954",
"name": "Phosphorylated GAB1 recruits PI3K to MET",
"equation": "",
"summary": "Phosphorylated tyrosine residues Y447, Y472 and Y589 of GAB1 are docking sites for the regulatory subunit PIK3R1 of the phosphatidyl inositol-3 kinase (PI3K) complex (Rodrigues et al. 2000). GAB1, phosphorylated by MET, thus recruits PI3K to activated MET (Schaeper et al. 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8851954",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8851954"
}
]
},
{
"id": "R-HSA-8852019",
"name": "MET bound PI3K generates PIP3",
"equation": "",
"summary": "Phosphatidylinositol-4,5-bisphosphate 3-kinase, PI3K, recruited to activated receptor tyrosine kinases such as EGFR (Rodrigues et al. 2000) and MET (Schaeper et al. 2000) via GAB1, catalyzes phosphatidylinositol-3,4,5-triphosphate (PIP3) synthesis, triggering downstream signaling by AKT family kinases.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8852019",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8852019"
}
]
},
{
"id": "R-HSA-8865994",
"name": "GAB1 binds PTPN11",
"equation": "",
"summary": "Phosphorylated tyrosine residues Y627 and Y659 of GAB1 serve as docking sites for the N-terminal and C-terminal SH2 domains of PTNP11 (SHP2), respectively, thus recruiting PTNP11 to the activated MET receptor (Schaeper et al. 2000, Cunnick et al. 2001). During mouse embryonic development, Gab1-mediated recruitment of Ptpn11 is crucial for Met receptor-directed placental development and migration of muscle progenitor cells to the limbs (Schaeper et al. 2007). PTPN11 is phosphorylated in response to HGF treatment, although phosphorylation sites and direct MET involvement have not been examined (Duan et al. 2006). Phosphorylation of PTPN11 at tyrosine residues Y542 and Y580 of splicing isoform 2 (matching Y546 and Y584 of PTPN11 splicing isoform 1) is required for PTPN11 phosphatase activity and for the recruitment of downstream effectors, such as GRB2 (Lu et al. 2001). Phosphorylation of PTPN11 in response to HGF treatment is required for the recruitment and activation of sphingosine kinase SPHK1, which may play a role in HGF-induced cell scattering (Duan et al. 2006). While PTPN11 promotes MAPK3/1 (ERK1/2) signaling downstream of MET, it can also dephosphorylate MET on unidentified tyrosine residues (Furcht et al. 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q06124-2",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8865994",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8865994"
}
]
},
{
"id": "R-HSA-8874078",
"name": "PTK2 autophosphorylates",
"equation": "",
"summary": "Binding to activated MET promotes PTK2 (FAK1) autophosphorylation at tyrosine residue Y397, a step involved in HGF-triggered cell migration (Chen and Chen 2006). It was demonstrated that PTK2 may associate with activated MET as a homodimer and that autophosphorylation at Y397 of PTK2 may happen in trans (Brami-Cherrier et al. 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05397-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8874078",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8874078"
}
]
},
{
"id": "R-HSA-8874079",
"name": "PTK2 binds activated MET",
"equation": "",
"summary": "PTK2 (FAK1) protein tyrosine kinase binds to activated MET receptor through the interaction of the FERM domain of PTK2 and phosphorylated tyrosine residues p-Y1349 and p-Y1356 of MET (Chen and Chen 2006). HGF-mediated activation of PTK2 requires interaction of integrins with the extracellular matrix components: collagen, laminin and fibronectin. HGF-mediated activation of MET causes extensive formation of new focal adhesions that contain PTK2 (Beviglia and Kramer 1999). Paxillin may also be involved in this interaction (Parr et al. 2001).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05397-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8874079",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8874079"
}
]
},
{
"id": "R-HSA-8874080",
"name": "SRC phosphorylates PTK2",
"equation": "",
"summary": "SRC phosphorylates PTK2 (FAK1) at tyrosine residues Y576 and Y577 in the activation loop of PTK2. Phosphorylation of PTK2 at Y576 and Y577 is required for the full catalytic activity of PTK2 (Calelb et al. 1995, Lietha et al. 2007) and is facilitated by MET-mediated phosphorylation of PTK2 at Y194. MET is able to phosphorylate PTK2 at Y576 and Y577 in vitro, in the absence of SRC (Chen et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q05397-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8874080",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8874080"
}
]
},
{
"id": "R-HSA-8874082",
"name": "MET phosphorylates PTK2",
"equation": "",
"summary": "Activated MET phosphorylates PTK2 (FAK1) at tyrosine residue Y194. Phosphorylation of PTK2 at Y194 facilitates SRC-mediated phosphorylation of PTK2 at Y577, but it has not been tested whether MET-mediated phosphorylation precedes SRC binding. MET may also phosphorylate PTK2 at Y5, although no functional significance of Y5 phosphorylation has been demonstrated. Activated EGFR and PDGFR can also phosphorylate PTK2 at Y5 and Y194 (Chen et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q05397-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8874082",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8874082"
}
]
},
{
"id": "R-HSA-8874083",
"name": "p-Y397-PTK2 binds SRC",
"equation": "",
"summary": "Phosphorylated tyrosine Y397 in the FERM domain of PTK2 (FAK1), along with an adjacent proline-rich motif, creates a docking site for the SRC kinase (Schaller et al. 1994, Xing et al. 1994, Thomas et al. 1998). It has not been specifically tested in this context whether PTK2 promotes SRC activation, and SRC is therefore represented in its active form.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q05397-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8874083",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8874083"
}
]
},
{
"id": "R-HSA-8874685",
"name": "CBL binds MET",
"equation": "",
"summary": "The E3 ubiquitin ligase CBL can bind to the MET receptor either indirectly, through GRB2, or directly, through phosphorylated tyrosine Y1003 of MET (Peschard et al. 2001, Taher et al. 2002, Peschard et al. 2004). The kinase responsible for Y1003 phosphorylation is not known. Y1003 has not been reported as a MET autophosphorylation site, and is implicated as a possible PKC-alpha target (Zhao et al. 2013). As CBL-mediated ubiquitination of MET happens in response to HGF stimulation (Taher et al. 2002, Abella et al. 2005), it is likely that MET autophosphorylation precedes MET phosphorylation at Y1003.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22681-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8874685",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8874685"
}
]
},
{
"id": "R-HSA-8875183",
"name": "CBL monoubiquitinates activated MET",
"equation": "",
"summary": "CBL monoubiquitinates activated MET receptor probably at multiple lysine residues, triggering MET endocytosis and degradation through the lysosomal route (Abella et al. 2005, Veiga and Cossart 2005). InlB, a cell wall protein of Listeria monocytogenes, binds to MET receptor as an HGF agonist. The subsequent CBL-mediated monoubiquitination of MET promotes endocytosis of bacteria and entry of Listeria monocytogenes into host cells (Veiga and Cossart 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22681-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875183",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875183"
}
]
},
{
"id": "R-HSA-8875371",
"name": "InlB binds MET",
"equation": "",
"summary": "InlB, a cell wall protein of Listeria monocytogenes, binds MET receptor, acting as an HGF agonist. InlB interacts with the extracellular portion of MET via two interfaces: the leucine rich repeat region (LRR) of InlB interacts with the Ig1 repeat of MET, while the inter-repeat (IR) region of InlB interacts with the Sema domain of MET (Shen et al. 2000, Veiga and Cossart 2005, Niemann et al. 2007).",
"cellular_location": "plasma membrane, peptidoglycan-based cell wall",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875371",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875371"
}
]
},
{
"id": "R-HSA-8875374",
"name": "MET binds LRIG1",
"equation": "",
"summary": "LRIG1 can bind the MET receptor in the absence of HGF-mediated MET activation and trigger MET downregulation in a CBL-independent manner (Shattuck et al. 2007). MET targeting by the therapeutic antibody SAIT301 leads to LRIG1-mediated MET degradation through the lysosomal route. LRIG1-mediated MET downregulation requires ubiquitination of LRIG1 by an unknown ubiquitin ligase and can be inhibited by the ubiqitin hydrolase USP8, which deubiquitinates LRIG1 (Oh et al. 2014, Lee et al. 2014). Ubiquitinated LRIG1 binds to HGS (Hrs), a protein involved in clathrin-mediated endocytosis, and LRIG1 and MET co-localize with the lysosomal marker LAMP1 (Oh et al. 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875374",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875374"
}
]
},
{
"id": "R-HSA-8875431",
"name": "LRIG1 undergoes ubiquitination",
"equation": "",
"summary": "Upon binding to MET, LRIG1 undergoes ubiquitination by an unknown ubiquitin ligase (Oh et al. 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875431",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875431"
}
]
},
{
"id": "R-HSA-8875443",
"name": "USP8 deubiquitinates LRIG1",
"equation": "",
"summary": "The ubiquitin hydrolase USP8 can deubiquitinate LRIG1, thus interfering with LRIG1-mediated MET downregulation (Oh et al. 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P40818-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875443",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875443"
}
]
},
{
"id": "R-HSA-8875451",
"name": "MET phosphorylates CBL",
"equation": "",
"summary": "MET phosphorylates CBL on unknown tyrosine residues. This is thought to precede CBL-mediated MET ubiquitination and may promote stronger interaction of CBL with the activated MET receptor complex (Peschard et al. 2001, Petrelli et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22681-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875451",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875451"
}
]
},
{
"id": "R-HSA-8875482",
"name": "CBL recruits CIN85:endophilin to ubiquitinated MET",
"equation": "",
"summary": "CBL recruits the complex of SH3KBP1 (CIN85) and endophilin to the activated MET receptor. While CIN85 and endophilin are not involved in CBL tyrosine phosphorylation by activated MET and CBL-mediated MET ubiquitination, they are required for internalization and degradation of the activated MET receptor (Petrelli et al. 2002). CIN85 likely functions as a homotetramer (Watanabe et al. 2000). Endophilin A1 (SH3GL2), A2 (SH3GL1) and A3 (SH3GL3), which function as homodimers, can all be recruited to the activated MET receptor, with SH3GL3 being the most extensively studied (Petrelli et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22681-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875482",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875482"
}
]
},
{
"id": "R-HSA-8875490",
"name": "EPS15 and HGS bind ubiquitinated MET",
"equation": "",
"summary": "EPS15 and HGS (Hrs) both bind MET receptor ubiquitinated by CBL upon HGF stimulation. EPS15 and HGS, which together form a ternary complex with STAM proteins (Bache et al. 2003) are involved in activated MET receptor endocytosis and degradation through the lysosomal route (Hammond et al. 2003). EPS15 can simultaneously interact with ubiquitinated MET and MET-bound GRB2 (Parachoniak et al. 2009). HGS also binds to ubiquitinated LRIG1 and is involved in LRIG1-trigerred lysosomal downregulation of MET in the absence of HGF stimulation (Oh et al. 2014). MET phosphorylates EPS15, HGS and STAM, but the functional significance of this phosphorylation for MET downregulation is not known (Row et al. 2005, Parachoniak et al. 2009).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22681-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875490",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875490"
}
]
},
{
"id": "R-HSA-8875523",
"name": "MET binds TNS3",
"equation": "",
"summary": "Activated MET receptor binds to tensin-3 (TNS3). The functional role of this interaction is not known. TNS3 is downregulated in colorectal, lung, ovarian and gastric cancers that show upregulation of tensin-4 (TNS4) (Muharram et al. 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q68CZ2-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875523",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875523"
}
]
},
{
"id": "R-HSA-8875531",
"name": "MET binds TNS4",
"equation": "",
"summary": "Activated MET receptor binds the complex of tensin-4 (TNS4) and integrin beta-1 (ITGB1). This interaction involves arginine residue R474 at the SH2 domain of TNS4 and phosphorylated tyrosines Y1349 and Y1356 of MET. Phosphorylated Y1313 of MET contributes to TNS4 binding but the kinase responsible for phosphorylation of MET at Y1313 is not known. TNS4, ITGB1 and MET co-localize at paxillin-positive focal adhesion sites. Binding of MET to TNS4 contributes to cell motility and promotes activation of AKT, but not ERK, downstream of MET. TNS4 is upregulated in colorectal, lung, ovarian and gastric cancer, with concomitant downregulation of TNS3. TNS4 and MET expression correlate in colorectal and ovarian cancer (Muharram et al. 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875531",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875531"
}
]
},
{
"id": "R-HSA-8875540",
"name": "GAB1 recruits CRK,CRKL to MET",
"equation": "",
"summary": "Splicing isoforms of adapter protein CRK, CRK-1 (CRKI) and CRK-2 (CRKII), as well as the related adapter protein CRKL can be recruited to the activated MET receptor via association with tyrosine phosphorylated GAB1 (Garcia-Guzman et al. 1999, Schaeper et al. 2000, Sakkab et al. 2000, Lamorte et al. 2000, Lamorte et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875540",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875540"
}
]
},
{
"id": "R-HSA-8875558",
"name": "RAPGEF1 binds CRK,CRKL",
"equation": "",
"summary": "Once recruited to the activated MET receptor complex by binding to tyrosine phosphorylated GAB1, CRK or related CRKL bind the Rap guanine nucleotide exchange factor RAPGEF1 (C3G) (Sakkab et al. 2000, Lamorte et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875558",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875558"
}
]
},
{
"id": "R-HSA-8875568",
"name": "RAPGEF1 activates RAP1",
"equation": "",
"summary": "The level of activated (GTP-bound) RAP1 increases rapidly after HGF stimulation. The recruitment of RAPGEF1 (C3G) to CRK or CRKL bound to MET-phosphorylated GAB1 brings RAPGEF1 to the plasma membrane, where it can act on its substrate, RAP1, catalyzing guanine nucleotide exchange from GDP to GTP (Sakkab et al. 2000, Lamorte et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875568",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875568"
}
]
},
{
"id": "R-HSA-8875576",
"name": "CRK,CRKL recruits RAC1 GEF to activated MET",
"equation": "",
"summary": "Recruitment of CRK or related CRKL to MET-phosphorylated GAB1 results in increased level of activated RAC1 (RAC1:GTP), a necessary step in HGF-induced cell motility (Lamorte et al. 2002, Watanabe et al. 2006). DOCK7 was recently implicated as a RAC1 guanyl nucleotide exchange factor (GEF) recruited to activated MET receptor via GAB1. Binding of DOCK7 to GAB1-bound CRK or CRKL was proposed but has not been examined (Murray et al. 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875576",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875576"
}
]
},
{
"id": "R-HSA-8875591",
"name": "DOCK7 activates RAC1",
"equation": "",
"summary": "DOCK7, recruited to the activated MET receptor complex through GAB1 and, possibly, CRK or CRKL, stimulates guanyl nucleotide exchange on RAC1 from GDP to GTP, resulting in RAC1 activation and HGF-stimulated cell migration/invasion (Murray et al. 2014).
Activation of RAC1 in response to HGF stimulation was reported to depend on the endosomal protein RAB5 and RAC1 guanyl exchange factor (GEF) TIAM1 (Palamidessi et al. 2008).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P63000-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875591",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875591"
}
]
},
{
"id": "R-HSA-8875659",
"name": "RAB4:GTP promotes recycling of activated MET receptor to the plasma membrane",
"equation": "",
"summary": "RAB4 is needed for recycling of the activated MET receptor complex (Parachoniak et al. 2011).",
"cellular_location": "plasma membrane, recycling endosome membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P62330-1",
"P20338-1",
"P61018-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875659",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875659"
}
]
},
{
"id": "R-HSA-8875661",
"name": "GGA3 associates with activated MET receptor",
"equation": "",
"summary": "GGA3 associates with the activated MET receptor through the CRK adapter and the ARF6:GTP complex and co-localizes with the MET receptor at early endosome membranes. The mechanistic details of GGA3 recruitment to MET have not been elucidated. GGA3 promotes recycling of the activated MET receptor through a RAB4-positive endosomal compartment (Parachoniak et al. 2011).",
"cellular_location": "plasma membrane, recycling endosome membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P62330-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875661",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875661"
}
]
},
{
"id": "R-HSA-8875816",
"name": "STAT3 binds activated MET receptor",
"equation": "",
"summary": "The STAT3 transcription factor may bind, directly and indirectly, to activated MET. Direct binding of STAT3 involves phosphorylated tyrosine residue Y1356 of MET. Indirect binding of STAT3 to activated MET involves GAB1, but this interaction has not been studied in detail (Schaper et al. 1997, Boccaccio et al. 1998).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875816",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875816"
}
]
},
{
"id": "R-HSA-8875817",
"name": "MET phosphorylates STAT3",
"equation": "",
"summary": "Activated MET phosphorylates STAT3 at Y705, triggering STAT3 dimerization and nuclear translocation (Boccaccio et al. 1998, Zhang et al. 2002, Cramer et al. 2005). Endocytosis of MET and interaction with STAT3 at endosomes may be required for sustained STAT3 phosphorylation in response to HGF stimulation (Kermorgant and Parker 2008). Activated SRC may also contribute to phosphorylation of STAT3 at Y705. STAT3 may promote HGF transcription in a SRC-dependent way, but this autocrine HGF loop may be limited to breast cancer cells (Wojcik et al. 2006, Sam et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8875817",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8875817"
}
]
},
{
"id": "R-HSA-8876210",
"name": "InlB promotes MET dimerization",
"equation": "",
"summary": "Listeria monocytogenes InlB proteins dimerize through their leucine-rich repeat regions (LRRs), promoting dimerization of their associated MET receptors (Ferraris et al. 2010).",
"cellular_location": "plasma membrane, peptidoglycan-based cell wall",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8876210",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8876210"
}
]
},
{
"id": "R-HSA-8876230",
"name": "InlB:MET dimer trans-autophophorylates",
"equation": "",
"summary": "MET bound to Listeria monocytogenes InlB protein undergoes trans-autophosphorylation. Phosphorylation at tyrosine residues Y1234 and Y1235 in the activation loop of the kinase domain of MET was specifically demonstrated. As InlB-activated MET activates downstream signaling by ERKs (MAPKs) and PI3K/AKT, MET is presumably phosphorylated on GRB2 and GAB1 docking sites Y1349 and Y1356, respectively (Niemann et al. 2007, Ferraris et al. 2010).",
"cellular_location": "cytosol, plasma membrane, peptidoglycan-based cell wall",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8876230",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8876230"
}
]
},
{
"id": "R-HSA-8876240",
"name": "CBL binds InlB-activated MET",
"equation": "",
"summary": "GRB2 is needed for the recruitment of CBL to the complex of Listeria monocytogenes InlB protein and phosphorylated MET receptor (Veiga and Cossart 2005).",
"cellular_location": "cytosol, plasma membrane, peptidoglycan-based cell wall",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22681-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8876240",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8876240"
}
]
},
{
"id": "R-HSA-8876246",
"name": "InlB-activated MET phosphorylates CBL",
"equation": "",
"summary": "Binding of InlB to MET receptor induces CBL phosphorylation on tyrosine residue(s). Based on the analogy with HGF-induced MET signaling, MET receptor activated by binding of the Listeria monocytogenes protein InlB phosphorylates CBL, promoting stronger interaction of CBL with MET (Peschard et al. 2001, Petrelli et al. 2002).",
"cellular_location": "cytosol, plasma membrane, peptidoglycan-based cell wall",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22681-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8876246",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8876246"
}
]
},
{
"id": "R-HSA-8876255",
"name": "CBL recruits CIN85:endophilin complex to InlB-bound MET",
"equation": "",
"summary": "CIN85 is necessary for endocytosis-mediated entry of Listeria monocytogenes triggered by CBL-mediated monoubiquitination of MET receptor activated by binding to the bacterial cell wall protein InlB (Veiga et al. 2005). Based on the analogy with HGF-activated MET signaling (Petrelli et al. 2002), CBL recruits the complex of CIN85 and endophilin to Listeria-engaged MET.",
"cellular_location": "cytosol, plasma membrane, peptidoglycan-based cell wall",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22681-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8876255",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8876255"
}
]
},
{
"id": "R-HSA-8876258",
"name": "CBL monoubiquitinates InlB-bound MET",
"equation": "",
"summary": "CBL promotes monoubiquitination of MET receptor that is activated by binding of the Listeria monocytogenes cell wall protein InlB. CBL-mediated monoubiquitination of MET promotes endocytosis and entry of Listeria monocytogenes into host cells (Veiga and Cossart 2005).",
"cellular_location": "cytosol, plasma membrane, peptidoglycan-based cell wall",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22681-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8876258",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8876258"
}
]
},
{
"id": "R-HSA-8876262",
"name": "EPS15 and HGS bind CBL-monoubiquitinated MET engaged with Listeria InlB",
"equation": "",
"summary": "Proteins involved in clathrin-mediated endocytosis EPS15 and HGS (Hrs) are both necessary for CBL and MET-mediated entry of Listeria monocytogenes into host cells (Veiga and Cossart 2005). Based on the analogy with HGF-activated MET signaling (Bache et al. 2003, Row et al. 2005, Parachoniak et al. 2009), HGS and EPS15, in complex with STAM proteins, bind to MET receptor monoubiquitinated by CBL upon MET receptor activation by the Listeria monocytogenes InlB protein.",
"cellular_location": "cytosol, plasma membrane, peptidoglycan-based cell wall",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22681-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8876262",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8876262"
}
]
},
{
"id": "R-HSA-8986940",
"name": "MET gene transcription is stimulated by MECP2",
"equation": "",
"summary": "MECP2 directly stimulates transcription of the MET gene, encoding MET receptor tyrosine kinase. MET promoter SNV rs1858830 C 'low activity' allele is associated with low expression of MET in autism spectrum disorders (ASD). Although this MET promoter SNV overlaps with the MECP2 binding site, presence of the low activity allele does not inhibit MECP2-mediated stimulation of MET transcription. Mutant MECP2 proteins associated with Rett syndrome show reduced transactivation of the MET gene. MET expression is significantly decreased in the temporal cortex of female Rett patients (Plummer et al. 2013).",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-9005531"
],
"output_participant_list": [
"R-HSA-419603"
],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8986940",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8986940"
}
]
},
{
"id": "R-HSA-9734070",
"name": "Anti-MET recombinant therapeutic antibodies bind MET",
"equation": "",
"summary": "Recombinant monoclonal anti-MET therapeutic antibodies are emerging as promising targeted therapeutics for the treatment of MET-driven cancers (reviewed in Comoglio et al. 2018).
Onartuzumab (also known as MetMAb), is an E. coli-derived humanized monovalent (one-armed) antibody that binds to MET and inhibits binding of HGF alpha chain to MET, thus preventing HGF-mediated activation of MET signaling. Onartuzumab does not display HGF agonism which is characteristic of some bivalent MET antibodies (Merchant et al. 2013).
Emibetuzumab (also known as LY2875358) is a humanized bivalent anti-MET monoclonal antibody which inhibits binding of HGF to MET and prevents HGF-mediate MET activation without exhibiting HGF agonism. In addition, emibetuzumab induces MET internalization and degradation, which further interferes with MET signaling (Liu et al. 2014).
ARGX-111 is an engineered anti-MET monoclonal antibody which competes with HGF for MET binding, acting as an HGF antagonist, inhibits HGF-induced MET activation, and engages natural killer cells to kill MET-expressing cancer cells, exhibiting enhanced antibody-dependent cellular toxicity (Hultberg et al. 2015).
SAIT301 is a bivalent recombinant anti-MET monoclonal antibody that likely acts as an HGF antagonist, but detailed studies are lacking. SAIT301 is thus annotated as a candidate HGF antagonist. SAIT301 inhibits activation of MET signaling by HGF and induces MET degradation that is independent of the MET E3 ubiquitin ligase CBL (Lee, Kim et al. 2014; Lee, Kang et al. 2014).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-9734070",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9734070"
}
]
},
{
"id": "R-HSA-9735946",
"name": "Anti-MET small tyrosine kinase inhibitors bind MET",
"equation": "",
"summary": "Several tyrosine kinase inhibitors (TKIs) have MET as their primary target. The majority of these TKIs act by competing with ATP for binding to the ATP binding pocket in the catalytic cleft of MET, thus inhibiting HGF-induced trans autophosphorylation and activation of MET homodimers, but some do not compete with ATP binding and instead act as allosteric inhibitors. In addition, several TKIs designed for other tyrosine kinases bind MET as their non primary target (reviewed in Comoglio et al. 2018).
TKIs whose primary target is MET are:
AMG-337: an ATP competitive inhibitor, highly specific for MET (Hughes et al. 2016);
amuvatinib (also known as MP470): an ATP competitive inhibitor of MET, KIT and AXL (Mahadevan et al. 2007); inhibits MET trans-autophosphorylation in response to HGF stimulation (Phillip et al. 2013); annotated as a candidate MET inhibitor due to insufficient availability of experimental data;
BMS-777607: an ATP competitive MET inhibitor (Schroeder et al. 2009); also inhibits MST1R (also known as RON) (Zeng et al. 2014);
cabozantinib (also known as XL184): an ATP comptetitive inhibitor of MET, KDR, KIT, RET, AXL, TEK and FLT3 (Yakes et al. 2011), acts by inhibiting trans-autophosphorylation of MET (Yakes et al. 2011, Xiang et al. 2014), thus interfering with HGF induced cell migration (Yakes et al. 2011); can increase the efficacy of other anti cancer drugs by inhibiting the action of the ATP dependent xenobiotic transporter ABCG2 (Zhang et al. 2017);
capmatinib (also known as IN280): an ATP competitive reversible inhibitor of MET (Liu et al. 2011);
crizotinib (also known as PF-2341066): an ATP competitive MET inhibitor (Zou et al. 2007)
foretinib (also known as XL2880 and GSK1363089): an ATP competitive inhibitor of MET; also inhibits KDR, KIT, MST1R, FLT1, FLT4, AXL and TEK (Qian et al. 2009, Kataoka et al. 2012);
glesatinib (also known as MGCD265): does not compete with ATP, but inhibits HGF dependent MET trans-autophosphorylation; is effective against MET exon 14 mutants that are resistant to ATP competitive inhibitors (Engstrom et al. 2017);
golvatinib (also known as E7050): a dual inhibitor of MET and KDR (Nakagawa et al. 2010)
MK-2461: an ATP competitive MET inhibitor; does not prevent HGF induced trans-autophosphorylation of the MET kinase activation loop, but prevents trans-autophosphorylation of the juxtamembrane domain and C terminal docking sites of MET (Pan et al. 2010); besides inhibiting MET, MK-2461 shows a similar potency against MST1R (RON) and FLT1 receptor tyrosine kinases (RTKs), and 8- to 30-fold lower potency against RTKs FGFR1, FGFR2, FGFR3, PDGFRB, KDR, FLT3, FLT4, NTRK1 (TRKA) and NTRK2 (TRKB);
OMO-1, annotated as a candidate due to insufficient published evidence; OMO-1 is an ATP competitive MET inhibitor (Libouban et al. 2018 - conference abstract, no data shown) that interferes with MET trans-autophosphorylation in response to HGF stimulation (Steenbrugge et al. 2021);
PHA-665752: an ATP competitive inhibitor of MET, inhibits HGF induced trans-autophosphorylation of MET and downstream cell proliferation and motility (Christensen et al. 2003);
savolitinib (also known as volitinib or AZD6094): an ATP competitive MET inhibitor (Jia et al. 2014, Gavine et al. 2015);
SGX-523: an ATP competitive, highly selective MET inhibitor; stabilizes MET in a unique inactive conformation, inaccessible to other protein kinases; abrogates HGF induced MET trans-autophosphorylation (Buchanan et al. 2009);
SU11274: an ATP competitive, selective MET inhibitor (50 times higher affinity for MET than other tested RTKs) (Sattler et al. 2003);
tepotinib: an ATP competitive MET inhibitor (Zhang et al. 2019);
tivantinib (also known as ARQ-197) is annotated as a candidate MET inhibitor because of contradicting evidence; it was initially found that tivantinib does not compete with ATP and acts as an allosteric inhibitor, diminishing trans-autophosphorylation of ligand-activated MET dimers (Munshi et al. 2010), but this could not be reproduced by Basilico et al. 2013; the study by Basilico et al. 2013. indicated that tivantinib displays a nonspecific, MET-independent cytotoxic effect by perturbing microtubule dynamics (Basilico et al. 2013); tivantinib is subject to multi drug resistance-related export via ATP-dependent xenobiotic transporter ABCG2 (Wu et al. 2020).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-9735946",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9735946"
}
]
}
],
"reaction_participants": [
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"participant_id": "R-HSA-419603",
"participant_name": "MET [plasma membrane]",
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},
{
"id": "DOID:10534",
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"name": "gastric neoplasm",
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},
{
"id": "MONDO:0001056",
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