Specifically, activated EPHA4 was shown to form a complex with FYN and LYN kinases (Prevost et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"P29323-1",
"Q5JZY3-1",
"P54764-1",
"P54760-1",
"P29317-1",
"P29322-1",
"P54753-1",
"P54756-1",
"P54762-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928584",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928584"
}
]
},
{
"id": "R-HSA-3928602",
"name": "NGEF binds EPHA",
"equation": "",
"summary": "Ephexin1/NGEF (Neuronal guanine nucleotide exchange factor) is a member of the Dbl family of guanine nucleotide exchange factors (GEFs) for Rho GTPases, which interacts with cytoplasmic domain of EPHAs. NGEF is highly expressed in the CNS during development and is enriched in neuronal growth cones. NGEF binds to the kinase domain of EPHA through its Dbl homology (DH)-pleckstrin-homology (PH) domains and this binding does not require activation of the receptor. EPHA activation by ephrinA ligands increases the catalytic activity of ephexin1 resulting in enhanced RHOA activation in cortical neurons (Noren & Pasquale 2004, Shamah et al. 2001). Ephrin-A1 also induces the dispersal of acetylcholine receptors clusters at the neuromuscular junction through the activation of NGEF and RhoA (Shi et al., 2010). NGEF is involved in both axonal growth,growth cone collapse, dendritic spine elimination and stabilization of the neuromuscular junction. In the absence of ephrin stimulation, NGEF promotes actin polymerization and axonal growth by stimulating RHOA, RAC1 and CDC42. Whereas in the presence of ephrin stimulation, NGEF induces growth cone collapse by activating RHOA, but not RAC1 and CDC42 (Shamah et al. 2001, Sahin et al. 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"Q5JZY3-1",
"P54764-1",
"P29317-1",
"P29322-1",
"P54756-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928602",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928602"
}
]
},
{
"id": "R-HSA-3928604",
"name": "SFKs phosphorylate VAV2,3",
"equation": "",
"summary": "Upon ephrin (EFN)-mediated stimulation, proto-oncogene vav (VAV) is transiently tyrosine phosphorylated and activated in neurons, possibly by Src family kinases (SFKs). VAV2 and VAV3 are phosphorylated on Y172 and Y173 respectively in the acidic domain and this phosphorylation disrupts the inhibitory interaction of the acidic domain with the DH domain (Cowan et al. 2005, Marignani & Carpenter 2001).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"P29323-1",
"Q5JZY3-1",
"P54764-1",
"P54760-1",
"P29317-1",
"P29322-1",
"P54753-1",
"P54756-1",
"P54762-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928604",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928604"
}
]
},
{
"id": "R-HSA-3928607",
"name": "p-EPHs bind VAV2,3",
"equation": "",
"summary": "The alternate method required for the initial EPH receptor:ephrin (EPH:EFN) adhesion into repulsion is by RAC-dependent endocytosis, an atypical endocytic mechanism by which the EPH:EFN complex and surrounding plasma membrane are internalized into one cell. Proto-oncogene vavs (VAVs) provide a molecular link between activated EPHs and RAC-dependent endocytosis. Upon the activation of EPH receptor, VAV proteins are recruited to the intracellular domain of EPHs and become transiently activated. Cowan et al. showed that VAV2 interacts with either EPHA4 or EPHB2, indicating that VAV can bind to either EPHA or EPHB subclass receptors. Autophosphorylated juxta-membrane tyrosines (Y596 and Y602 of human EPHA4) provide docking sites for VAV proteins (Cowan et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"P29323-1",
"Q5JZY3-1",
"P54764-1",
"P54760-1",
"P29317-1",
"P29322-1",
"P54753-1",
"P54756-1",
"P54762-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928607",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928607"
}
]
},
{
"id": "R-HSA-3928623",
"name": "EPHBs bind NMDARs",
"equation": "",
"summary": "EPHBs are involved in spine synapse formation and also for the recruitment and clustering of glutamate receptors to synapses. At the time of synaptogenesis, EPHBs are localized to the postsynaptic region of excitatory synapses. These postsynaptic EPHBs, upon activation by presynaptic ephrinBs (EFNBs), directly interact with ionotropic glutamate receptor, NR1 and NR2B (NMDAR1and 2B aka GRIN1and 2B). The interaction between EPHB and NMDARs is mediated by the extracellular domains of these two proteins. This interaction promotes clustering of NMDARs at synaptic locations and leads to the formation of functional presynaptic release sites. Activated EPHBs function as tyrosine kinases and may also indirectly potentiate NMDAR-mediated calcium influx (Dalva et al. 2000, Takasu et al. 2002).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07947-1",
"P07948-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928623",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928623"
}
]
},
{
"id": "R-HSA-3928627",
"name": "EPHB phosphorylates TIAM1",
"equation": "",
"summary": "Once recruited to the EPHB:NMDAR complex, T-lymphoma invasion and metastasis-inducing protein 1 (TIAM1) is phosphorylated on tyrosine 829 by either EPHB or a kinase that associates with activated EPHB. TIAM1 may then activate Rac1, leading to actin cytoskeletal remodelling required for spine development and morphogenesis (Tolias et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07947-1",
"P07948-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928627",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928627"
}
]
},
{
"id": "R-HSA-3928628",
"name": "VAV exchanges GTP for GDP on RAC1, activating it",
"equation": "",
"summary": "Activated proto-oncogene vav (VAV) act as guanine nucleotide exchange factors (GEFs) for RAC1, catalysing the exchange of bound GDP for GTP. Endocytosis of large EPH:EFN complexes is dependent on RAC1-regulated actin polymerization. RAC1 signaling is positively linked to EPH:EFN internalization but the exact link to clathrin endocytosis machinery remains unclear. Inhibiting RAC1 signalling and Arp2/3-driven actin polymerization in EPH receptor-expressing cells completely blocks both endocytosis of EPH:EFN complexes and cell retraction (Marston et al. 2003). In response to repulsive guidance molecules, the function of RAC1 changes from promoting actin polymerization associated with axon growth to driving endocytosis of the plasma membrane, resulting in growth cone collapse (Jurney et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P63000-1",
"P07947-1",
"P07948-1",
"P29320-1",
"P29323-1",
"Q5JZY3-1",
"P54764-1",
"P54760-1",
"P29317-1",
"P29322-1",
"P54753-1",
"P54756-1",
"P54762-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928628",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928628"
}
]
},
{
"id": "R-HSA-3928642",
"name": "TIAM1 exchanges GTP for GDP on RAC1, activating it",
"equation": "",
"summary": "Activation of EPH receptors triggers the local activation of T-lymphoma invasion and metastasis-inducing protein 1 (TIAM1) and this in turn activates RAC1 (Yoo et al. 2010). RAC1 signaling is positively linked to EPH:ephrin (EFN) internalization but the exact link to clathrin endocytosis machinery remains unclear. TIAM1 co-localizes with the ARP2/3 complex at sites of actin polymerization. RAC1 activated by TIAM1 then subsequently activates the ARP2/3 complex proteins leading to actin polymerization (Ten Klooster et al. 2006).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P63000-1",
"P07947-1",
"P07948-1",
"P29320-1",
"Q5JZY3-1",
"P54764-1",
"P29317-1",
"P29322-1",
"P54756-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928642",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928642"
}
]
},
{
"id": "R-HSA-3928645",
"name": "EPHB:NMDAR binds TIAM1",
"equation": "",
"summary": "T-lymphoma invasion and metastasis-inducing protein 1 (TIAM1) is a Rac1-specific GEF, highly expressed in the nervous system, which is necessary for proper spinal and synapse development. It is one of the critical mediators of NMDA receptor (NMDAR)-dependent spine development (Tolias et al. 2005). TIAM1 might also play a role in regulating EPHB-dependent spine morphogenesis. TIAM1 appears to be required for ephrinB (EFNB)-induced increase in spine density. TIAM1 is recruited to EPHB complexes containing NMDAR after EPHB receptor activation in neurons. The PH-CC-Ex (consisting of a pleckstrin homology (PH) domain followed by a coiled-coiled (CC) domain and an adjacent region (Ex) domain) of TIAM1 is required for binding to EPHB2 (Tolias et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07947-1",
"P07948-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928645",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928645"
}
]
},
{
"id": "R-HSA-3928648",
"name": "SFKs phosphorylate NGEF",
"equation": "",
"summary": "Activation of EPHAs leads to phosphorylation of ephexin1 (NGEF) on conserved tyrosine (Y) 179 (Y87 in isoform3) by Src family kinases (SFKs). This phosphorylation preferentially activates NGEF\u2019s GDP/GTP exchange activity specifically towards RHOA but not RAC1 and CDC42, thus switching the substrate preference of NGEF and leading to actin cytoskeletal changes that result in growth cone collapse (Sahin et al. 2005, Knoll and Drescher 2004).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"Q5JZY3-1",
"P54764-1",
"P29317-1",
"P29322-1",
"P54756-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928648",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928648"
}
]
},
{
"id": "R-HSA-3928651",
"name": "NGEF exchanges GTP for GDP on RHOA",
"equation": "",
"summary": "The tyrosine phosphorylation of ephexin1 (NGEF)/Ephexin-1 enhances its exchange activity and specifically activates inactive RHOA:GDP to active RHOA:GTP. Activated RHOA regulates myosin II activity in neurons through Rho-associated kinase (ROCK), and leads to rapid growth cone collapse, neurite retraction, or neurite growth inhibition in axons. Through this repulsive mechanism EPH receptors and ephrins (EFNs) guide retinal axons to their targets in the visual centres in the brain (Sahin et al. 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P61586-1",
"P29320-1",
"Q5JZY3-1",
"P54764-1",
"P29317-1",
"P29322-1",
"P54756-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928651",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928651"
}
]
},
{
"id": "R-HSA-4093327",
"name": "EPHA binds TIAM1",
"equation": "",
"summary": "T-lymphoma invasion and metastasis-inducing protein 1 (TIAM1) is a GEF exhibiting highest specificity for RAC1 and is critically involved in EPH/ephrin (EFN)-mediated neurite outgrowth and dendritic spine development (Tanaka et al. 2004, Tolias et al. 2007). TIAM1 has a role in regulating the endocytosis of EPHA receptors, by regulating the RAC1 signaling downstream of the EPHA8 receptor. Yoo and his colleagues found that TIAM1, a RAC-specific guanine nucleotide exchange factor, co-immunoprecipitates with EPHA8 in response to EFNA5 stimulation. TIAM1 associates with EPHA8 in the juxtamembrane (JM) region. Deletion of the JM region or down-regulation of TIAM1 expression compromises EPHA8:EFNA5 endocytosis (Yoo et al. 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"Q5JZY3-1",
"P54764-1",
"P29317-1",
"P29322-1",
"P54756-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-4093327",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4093327"
}
]
},
{
"id": "R-HSA-4093336",
"name": "p-TIAM1 exchanges GTP for GDP on RAC1, activating it",
"equation": "",
"summary": "Phosphorylated T-lymphoma invasion and metastasis-inducing protein 1 (p-TIAM1) bound to EPHB complexes containing NMDARs, promotes spine morphogenesis by activating RAC1, which triggers actin cytoskeletal remodelling that is essential for spine development (Tolias et al. 2007, Tolias et al. 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"P07947-1",
"P07948-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-4093336",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4093336"
}
]
},
{
"id": "R-HSA-432295",
"name": "GPVI binds Fyn and Lyn",
"equation": "",
"summary": "Fyn and Lyn constitutively associate with GPVI-Fc epsilon R1 gamma in platelets. The proline-rich region of GPVI is required for this interaction.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-432295",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-432295"
}
]
},
{
"id": "R-HSA-437118",
"name": "GPVI stimulates PI3K beta, gamma",
"equation": "",
"summary": "GPVI downstream signaling involves PI3K. Mouse knockouts of PI3Kbeta/PI3Kgamma suggest that though both isoforms are required for a full platelet response, only beta is absolutely required for Akt phosphorylation, Rap1 activation, and platelet aggregation downstream. The pathway connecting GPVI to PI3K is unclear. Two possible routes are suggested by interactions of the PI3K p85 regulatory subunit with LAT and with peptides representing the ITAM motif of Fc Epsilon R1 gamma.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P48736-1",
"P06241-1",
"P07948-1",
"P43405-1",
"P42338-1"
],
"evidence": [
{
"id": "R-HSA-437118",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-437118"
}
]
},
{
"id": "R-HSA-453183",
"name": "p-Y348-SYK dissociates",
"equation": "",
"summary": "Structural and biophysical studies indicate that the adaptability of the Syk tandem SH2 domains is made possible by relatively weak interactions between the two SH2 domains and the flexibility of interdomain A (Zhang et al. 2008).; A large proportion of phosphorylated Syk is released into the cytosol. One factor that has been proposed for modulating the interactions of Syk with the receptor ITAM is the phosphorylation of Syk on Y130 (Keshvara et al. 1997).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07948-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-453183",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-453183"
}
]
},
{
"id": "R-HSA-453200",
"name": "SYK autophosphorylates",
"equation": "",
"summary": "Binding of Syk causes conformational changes that lead to Syk activation by autophosphorylation. Syk can be activated by a number of phosphorylation events, and it has been proposed that Syk may function as a switch whereby any of several possible stimuli trigger the acquisition of similar activated conformations. (Tsang et al. 2008). These phosphorylations both modulate Syk's catalytic activity (Keshvara et al. 1997) and generate docking sites for SH2 domain-containing proteins, such as c-Cbl, PLC, and Vav1. ; ; Syk tyrosine phosphorylation is reduced in the presence of the ITIM-containing immunoglobulin superfamily transmembrane protein G6B (Mori et al. 2008).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07948-1",
"Q06124-2",
"P43405-1",
"P29350-1"
],
"evidence": [
{
"id": "R-HSA-453200",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-453200"
}
]
},
{
"id": "R-HSA-5621355",
"name": "LYN and FYN phosphorylate FCER1G in CLEC6A:FCERG and CLEC4E:FCERG",
"equation": "",
"summary": "Ligation of CLEC6A (C-type lectin domain family 6 member A/Dectin-2) and CLEC4E (Mincle) with their appropriate ligands trigger the tyrosine phosphorylation of the immune receptor tyrosine-based activation motif (ITAM) in the cytoplasmic tail of FCER1G chain. Tyrosine Y65 and Y76 in the ITAM are phosphorylated and this phosphorylation is mediated by Src kinases Lyn and Fyn (Sato et al. 2006, Yamasaki et al. 2008, Quek et al. 1998).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-5621355",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5621355"
}
]
},
{
"id": "R-HSA-5624486",
"name": "SFKs phosphorylates RAF1 on Y340,Y341",
"equation": "",
"summary": "Phosphorylation of tyrosine 340, 341 (Y340,341) on RAF1 in response to CD209 (DC-SIGN) signalling depends on yet unidentified members of the Src family of tyrosine kinases (SFKs). In imunoprecipitation studies, CD209 from lipid rafts of dendritic cells was found to co-precipitate with LYN, a member of the SFK, as well as with SYK tyrosine kinase, indicating their possible involvement in DC-SIGN signalling (Caparros et al. 2006, Svajger et al. 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P06241-1",
"P04049-1",
"P07948-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-5624486",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5624486"
}
]
},
{
"id": "R-HSA-5690702",
"name": "LYN phosphorylates CD22",
"equation": "",
"summary": "After ligation of membrane-bound IgM, CD22 is quickly tyrosine phosphorylated on its cytoplasmic ITIM sequence (immunoreceptor tyrosine-based inhibition motif). The tyrosine kinase involved in CD22 phosphorylation is LYN, a member of the Src kinase family (Smith et al. 1998). The CD22 cytoplasmic tail contains six tyrosines, three of which belong to the ITIM sequence (Nitschke & Tsubata 2004).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-5690702",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5690702"
}
]
},
{
"id": "R-HSA-879917",
"name": "CBL, GRB2, FYN and PI3K p85 subunit are constitutively associated",
"equation": "",
"summary": "Cbl is constitutively associated with Grb2 in resting hematopoietic cells (Anderson et al. 1997, Odai et al. 1995, Park et al. 1998, Panchamoorthy et al. 1996). Both the SH2 and SH3 domains of Grb2 are involved. Cbl has 2 distinct C-terminal domains, proximal and distal. The proximal domain binds Grb2 in resting and stimulated cells, and in stimulated cells also binds Shc. The distal domain can bind the adaptor protein CRKL.
; Tyrosine phosphorylation of Cbl in response to IL-3 releases the SH3 domain of Grb2 which then is free to bind other molecules (Park et al. 1998).
Cbl also associates with Fyn (Anderson et al. 1997) and the related kinases Hck and Lyn (Hunter et al. 1999). Binding studies indicate that this binding is independent of the phosphorylation state of Cbl; The association of Fyn with Cbl has been described as constitutive (Hunter et al. 1999).
; Cbl further associates with the p85 subunit of PI3K (Hartley et al. 1995, Anderson et al. 1997, Hunter et al. 1997), this is also described as constitutive and is mediated by the SH3 domain of p85 (Hunter et al. 1997).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P22681-1",
"P07947-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-879917",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879917"
}
]
},
{
"id": "R-HSA-8942607",
"name": "Tyrosine kinases phosphorylate Cip/Kip inhibitors bound to CDK4/6:CCND complexes",
"equation": "",
"summary": "Phosphorylation of Cip/Kip cyclin-dependent kinase (CDK) inhibitors CDKN1A (p21Cip), CDKN1B (p27Kip1) and CDKN1C (p57Kip2) on conserved tyrosine residues Y77, Y88 and Y91, respectively, can convert them from bound inhbitors to bound non-inhibitors of CDK4 or CDK6 complexes with D cyclins by dislodging them from the active site of CDK4 or CDK6. This mechanism was studied in most detail on the example of CDKN1B associated with the CDK2:CCNA complex (Grimmler et al. 2007) and the CDK4:CCND1 complex (James et al. 2008, Patel et al. 2015). For a review of this topic, please refer to Blain 2008.
CDKN1A can be phosphorylated at tyrosine residue Y77 by protein tyrosine kinase ABL1 (Hukkelhoven et al. 2012). CDKN1B can be phosphorylated at tyrosine residue Y88, and probably also at the adjacent Y89, by protein tyrosine kinases ABL1 (Grimmler et al. 2007, James et al. 2008, Ray et al. 2009, Ou et al. 2011), LYN (Grimmler et al. 2007), SRC (Larrea et al. 2008), JAK2 (Jakel et al. 2011) and PTK6 (Patel et al. 2015). CDKN1C can be phosphorylated at tyrosine residue Y91 by protein tyrosine kinase ABL1 (Borriello et al. 2011).
Dislodgment of the tyrosine phosphorylated 3-10 helix of Cip/Kip CDK inhibitors from the active site of cyclin D-bound CDK4 or CDK6 results in increased catalytic activity of CDK4 or CDK6 by allowing ATP binding to the active site, but also by enabling activating phosphorylation of the T-loop of CDK4 or CDK6 phosphorylation by CDK7 in complex with cyclin H (Ray et al. 2009).
SRC-mediated phosphorylation of CDKN1B on tyrosine residue Y88 was shown to reduce protein stability of CDKN1B (Chu et al. 2007).
Without overexpression of BCR-ABL or SRC-family tyrosine kinases in several cell systems, tyrosine phosphorylated p27 is either undetectable or a very low abundance species (Ishida et al. 2000, Jaimes et al. 2008, Grimmler et al. 2007) that does not bind preferentially to CDK4 (Jaimes et al. 2008). Therefore, tyrosine phosphorylation of p27 is unlikely to be the sole explanation of the full activity of p27-bound CDK4:CCND complexes reported in previous studies (Blain et al. 1997, Coulonval et al. 2003, Bockstaele et al. 2006). It has been proposed that stoichiometry of the Cip/Kip complex with CDK4 or CDK6 and cyclin D, in addition to or alternative to tyrosine phosphorylation of Cip/Kip CDK inhibitors, determines their inhibitory role where binding of more than one molecule of CDKN1A, CDKN1B or CDKN1C would be needed to achieve inhibition of the CDK4/6:CCND complex (reviewed by Paternot et al. 2010).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13882-1",
"O60674-1",
"P00519-1",
"P07948-1",
"P11802-1",
"Q00534-1"
],
"evidence": [
{
"id": "R-HSA-8942607",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8942607"
}
]
},
{
"id": "R-HSA-9006323",
"name": "Phospho-JAK2 phosphorylates EPOR",
"equation": "",
"summary": "Phosphorylated JAK2 phosphorylates 8 tyrosine residues in the cytoplasmic tail of EPOR (Dusanter-Fourt et al. 1992, McGraw et al. 2012, and inferred from mouse homologs). The phosphorylated residues then serve as binding sites for scaffold proteins such as CRKL and GAB1 and downstream signaling proteins such as STAT5, phospholipase C, and phosphatidylinositol 3-kinase.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9006323",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9006323"
}
]
},
{
"id": "R-HSA-9006325",
"name": "EPO binds EPOR:JAK2:LYN:IRS2",
"equation": "",
"summary": "Extracellular Erythropoietin (EPO) binds the EPO receptor (EPOR) located in the plasma membrane of the target cell (Jones et al. 1990, Syed et al. 1998, Remy et al. 1999, and inferred from mouse homologs). EPOR is a dimer that appears to be preassociated with downstream signaling proteins JAK2 (inferred from mouse homologs) and LYN (Chin et al. 1998, and inferred from mouse homologs) and the scaffold protein IRS2 (Verdier et al. 1997). Binding of EPO to EPOR causes a change in the conformation of the dimer which activates JAK2 (Syed et al. 1998, Remy et al. 1999, Kubatzky et al. 2001).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9006325",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9006325"
}
]
},
{
"id": "R-HSA-9006332",
"name": "JAK2 transphosphorylates and is activated in response to Erythropoietin",
"equation": "",
"summary": "Upon binding EPO, the EPOR dimer changes conformation, resulting in activation of JAK2 associated with box 1 and box 2 of the cytoplasmic domain of each EPOR (inferred from mouse homologs). One JAK2 transphosphorylates 12 tyrosine residues of the other JAK2 thereby activating JAK2 to phosphorylate EPOR and other substrates (Arcasoy et al. 1999, Watowich et al. 1999, Erickson-Miller et al. 2000, and inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9006332",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9006332"
}
]
},
{
"id": "R-HSA-9012650",
"name": "JAK2 and LYN phosphorylate STAT5 in EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2",
"equation": "",
"summary": "After STAT5 binds the EPO:EPOR complex, phosphorylated JAK2 and LYN phosphorylate STAT5 (STAT5A or STAT5B) (Gouilleux et al. 1995, Pallard et al. 1995, Hoefsloot et al. 1997, Miura et al. 1998, Oda et al. 1998, Okajima et al. 1998, Erickson-Miller et al. 2000, and inferred from mouse homologs). STAT5A (MGH-STAT5) is phosphorylated on tyrosine-694 (Gouilleux et al. 1995, Arcasoy et al. 1999). Activation of STAT5 appears to be impaired in myelodysplastic syndrome (Hoefsloot et al. 1997). IGF-I enhances STAT5 phosphorylation in response to EPO (Okajima et al. 1998).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9012650",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9012650"
}
]
},
{
"id": "R-HSA-9012651",
"name": "p-STAT5 dissociates from EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2",
"equation": "",
"summary": "After being phosphorylated, phospho-STAT5 (STAT5A or STAT5B) dissociates from the EPO:EPOR complex, dimerizes, and transits to the nucleus where it activates transcription of target genes (Oda et al. 1998, and inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9012651",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9012651"
}
]
},
{
"id": "R-HSA-9012654",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 binds STAT5",
"equation": "",
"summary": "STAT5 (STAT5A or STAT5B) binds the phosphorylated cytoplasmic domain of EPOR via phosphotyrosine-343 and phosphotyrosine-479 of EPOR (Chretien et al. 1996, McGraw et al. 2012, and inferred from mouse homologs). STAT5 may also bind the EPOR complex indirectly via CRKL (Ota et al. 1998).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9012654",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9012654"
}
]
},
{
"id": "R-HSA-9012657",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:phospho-IRS2 binds PI3K",
"equation": "",
"summary": "Phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) binds phosphorylated IRS2 associated with the phosphorylated EPOR (Bouscary et al. 2003).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"O60674-1",
"P48736-1",
"P07948-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-9012657",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9012657"
}
]
},
{
"id": "R-HSA-9021627",
"name": "EPOR-associated PI3K phosphorylates PIP2 to PIP3",
"equation": "",
"summary": "Phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) associated with EPOR phosphorylates phosphatidylinositol 4,5-bisphosphate to yield phosphatidyl 3,4,5-trisphosphate (Kubota et al. 2001, Schmidt et al. 2004). PI3K binds the phosphorylated EPOR directly or indirectly via phosphorylated IRS2 or phosphorylated GAB1 (Bouscary et al. 2003).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"O60674-1",
"P48736-1",
"P07948-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-9021627",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9021627"
}
]
},
{
"id": "R-HSA-9024723",
"name": "EPO:p-EPOR:p-JAK2:LYN:IRS2 binds CRKL:RAPGEF1",
"equation": "",
"summary": "CRKL, in a constitutive complex with RAPGEF1 (C3G, a nucleotide exchange factor for RAP1), binds the cytoplasmic domain of EPOR in the region of phosphotyrosine-460 (Arai et al. 2001).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9024723",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9024723"
}
]
},
{
"id": "R-HSA-9024726",
"name": "LYN phosphorylates CRKL in EPO:p-8Y-EPOR:p-12Y-JAK2:LYN:IRS2:CRKL:RAPGEF1",
"equation": "",
"summary": "LYN, in a complex with EPOR, phosphorylates CRKL bound to RAPGEF1 (Arai et al. 2001).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9024726",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9024726"
}
]
},
{
"id": "R-HSA-9027272",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 phosphorylates IRS2",
"equation": "",
"summary": "IRS2 is constitutively associated with EPOR and is phosphorylated on tyrosine residues in response to EPO (Verdier et al. 1997, Bouscary et al. 2003). The phosphorylated IRS2 serves as a docking site for downstream signaling proteins, notably phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) (Bouscary et al. 2003).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9027272",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027272"
}
]
},
{
"id": "R-HSA-9027273",
"name": "JAK2 phosphorylates GAB1 in EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:GAB1",
"equation": "",
"summary": "Phosphorylated JAK2 in a complex with EPOR and GAB1 phosphorylates GAB1 on unknown tyrosine residues (Lecoq-Lafon et al. 1999, Wickrema et al. 1999, Bouscary et al. 2003, Fukumoto et al. 2009). Phosphorylated GAB1 serves as a scaffold for binding downstream signaling molecules including phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) (Bouscary et al. 2003).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9027273",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027273"
}
]
},
{
"id": "R-HSA-9027274",
"name": "EPO:p-8Y-EPOR:p-12Y-JAK2:LYN:IRS2:p-CRKL:RAPGEF1 binds SHC1",
"equation": "",
"summary": "After stimulation by EPO, CRKL associates with EPOR, is phosphorylated, and binds SHC1 (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9027274",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027274"
}
]
},
{
"id": "R-HSA-9027275",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-GAB1 binds PI3K",
"equation": "",
"summary": "Phosphorylated GAB1 in a complex with EPOR binds the p85 subunit of phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) (Lecoq-Lafon et al. 1999, Wickrema et al. 1999, Bouscary et al. 2003).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"O60674-1",
"P48736-1",
"P07948-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-9027275",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027275"
}
]
},
{
"id": "R-HSA-9027280",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 binds PI3K",
"equation": "",
"summary": "Phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) can directly bind phosphotyrosine-479 in the cytosolic domain of EPOR (Kubota et al. 2001, Bouscary et al. 2003, and inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"O60674-1",
"P48736-1",
"P07948-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-9027280",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027280"
}
]
},
{
"id": "R-HSA-9027281",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 binds GAB1",
"equation": "",
"summary": "GAB1 binds directly to phosphotyrosines 344 and 402 of the EPOR (Bouscary et al. 2003, Montoye et al. 2005). GAB1 can also indirectly bind the EPOR via SHC1 or GRB2. GAB2 is absent from human erythroid progenitors but present in mouse erythroid progenitors (Wickrema et al. 1999).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9027281",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027281"
}
]
},
{
"id": "R-HSA-9027373",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 binds PLCgamma",
"equation": "",
"summary": "PLCG2 (PLCgamma2) binds phosphotyrosine-432 and phosphotyrosine-480 of EPOR (Montoye et al. 2005, and inferred from moue homologs). PLCG1 can also bind the phosphorylated EPOR (inferred from mouse homologs). After binding, PLCG2 is phosphorylated (Ren et al. 1994)",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P19174-1",
"P07948-1",
"P16885-1"
],
"evidence": [
{
"id": "R-HSA-9027373",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027373"
}
]
},
{
"id": "R-HSA-9027425",
"name": "LYN phosphorylates PLCG1,2 in EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:PLCG1,2",
"equation": "",
"summary": "PLCG1 (Phospholipase C gamma1) or PLCG2 bound to the activated EPOR is phosphorylated on tyrosine residues by the kinase LYN (Ren et al. 1994, and inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P19174-1",
"P07948-1",
"P16885-1"
],
"evidence": [
{
"id": "R-HSA-9027425",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027425"
}
]
},
{
"id": "R-HSA-9029149",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-CRKL:RAPGEF1:phospho-SHC1 binds GRB2:SOS1",
"equation": "",
"summary": "Phosphorylated SHC1 in the EPOR complex serves as a scaffold to bind GRB2 bound to SOS1 (Damen et al. 1993, Odai et al. 1997). GRB2 may be pre-associated with VAV1 or SOS1, which are guanine nucleotide exchange factors for RAS, or with CBL, an ubiquitin ligase (Odai et al. 1997).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9029149",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9029149"
}
]
},
{
"id": "R-HSA-9029150",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-CRKL:RAPGEF1:phospho-SHC1 binds GRB2:VAV1",
"equation": "",
"summary": "Phosphorylated SHC1 in a complex with the activated EPOR binds GRB2 bound to VAV1 (Hanazono et al. 1995, Hanazono et al. 1996, Odai et al. 1997). GRB2 exists in pre-assembled complexes with VAV1 (Hanazono et al. 1995), SOS1 (Odai et al. 1997), or CBL (Odai et al. 1997). VAV1 and SOS1 are guanine nucleotide exchange factors that activate the RAS signaling pathway.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9029150",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9029150"
}
]
},
{
"id": "R-HSA-9029151",
"name": "JAK2 phosphorylates VAV1 in EPO:p-8Y-EPOR:p-12Y-JAK2:LYN:IRS2:p-Y-CRKL:RASGEF1:p-Y-SHC1:GRB2:VAV1",
"equation": "",
"summary": "Phosphorylated JAK2 phosphorylates VAV1 bound to GRB2 in a large complex assembled on the phosphorylated EPOR (Odai et al. 1997, Shigematsu et al. 1997). Phosphorylation of VAV1 activates its guanine nucleotide exchange activity (inferred from the mouse homolog).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9029151",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9029151"
}
]
},
{
"id": "R-HSA-9029155",
"name": "JAK2 phosphorylates SHC1 in EPO:p-8Y-EPOR:p-12Y-JAK2:LYN:p-CRKL:RABGEF1:SHC1",
"equation": "",
"summary": "Phosphorylated JAK2 associated with the EPOR complex phosphorylates SHC1 (Damen et al. 1993, Verma et al. 2014) bound to CRKL in the EPOR complex. The phosphorylated SHC1 serves as a scaffold to bind downstream effectors including GRB2:VAV1 and GRB2:SOS1.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9029155",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9029155"
}
]
},
{
"id": "R-HSA-9029158",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-CRKL:RAPGEF1:GRB2-1:SOS1,phospho-VAV1 mediates exchange of GTP for GDP bound to RAS",
"equation": "",
"summary": "SOS1 and phospho-VAV1 bound to GRB2 in a complex with the activated EPOR catalyze the exchange of GDP for GTP bound to RAS proteins, yielding RAS:GTP (Komatsu et al. 1992, Torti et al. 1992). RAS:GTP then activates RAF1 and ERK1 and ERK2. EPO is observed to activate HRAS (Komatsu et al. 1992, Torti et al. 1992), KRAS, and NRAS (inferred from mouse homologs). KRAS appears to be particularly important for erythropoiesis since deletion of KRAS causes anemia in mouse.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"P07948-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9029158",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9029158"
}
]
},
{
"id": "R-HSA-9032478",
"name": "EPOR-associated PLCG hydrolyzes 1-Phosphatidyl-1D-myo-inositol 4,5-bisphosphate",
"equation": "",
"summary": "Phospholipase C gamma (PLCG1 or PLCG2) bound to the phosphorylated cytoplasmic domain of the EPO receptor (EPOR) hydrolyzes 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to yield the second messengers diacylglycerol and 1D-myo-inositol 1,4,5-trisphosphate (Ren et al. 1994, and inferred from mouse). Erythropoietin may also activate the hydrolysis of phosphatidylcholine and phosphatidylethanolamine (inferred from mouse homologs),",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P19174-1",
"P07948-1",
"P16885-1"
],
"evidence": [
{
"id": "R-HSA-9032478",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9032478"
}
]
},
{
"id": "R-HSA-912627",
"name": "CBL ubiquitinates PI3K",
"equation": "",
"summary": "Cbl is an E3 ubiquitin-protein ligase that negatively regulates signaling pathways by targeting proteins for ubiquitination and proteasomal degradation (Rao et al. 2002). Cbl-B targets PI3K for ubiquitination and degradation in T cells (Fang et al. 2000). Similarly, Cbl activation by tyrosine phosphorylation increases PI3K ubiquitination and proteasomal degradation (Dufour et al. 2008).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P22681-1",
"P07947-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-912627",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912627"
}
]
},
{
"id": "R-HSA-912629",
"name": "CBL is tyrosine phosphorylated",
"equation": "",
"summary": "Cbl is tyrosine phosphorylated following stimulation with IL-3 (Anderson et al. 1997) and GM-CSF (Odai et al. 1995). Cbl may be phosphorylated prior to this IL-3 stimulated tyrosyl phosphorylation (Park et al. 1998). The kinase responsible for Cbl phosphorylation may be dependent on cell type; Fyn is demonstrated to have the ability to phosphorylate Cbl (Hunter et al. 1999), other candidates include Hck, Lyn (Hunter et al. 1999) and Syk (Park et al. 1998).
; Tyrosines 700, 731 and 774 are the major sites of Cbl phosphorylation by non-receptor protein tyrosine kinases, with none showing any particular specificity for sites (Tsygankov et al. 2001). Fyn was observed to be constitutively associated with Cbl in lysates of several different cell types including the interleukin-3-dependent murine myeloid cell line 32Dcl3, and the prolactin-dependent rat thymoma cell line Nb2. Cbl phosphorylation at Y731 is postulated to provide an additional interaction between Cbl and the SH2 domain of p85-PI3K (Hunter et al. 1999). Cbl-p85 association increases in activated cells (Panchamoorthy et al. 1996). Expression of a Cbl Y731F mutant which abolishes binding of Cbl to p85 markedly increased levels of p85-PI3K (Dufour et al. 2008). Cbl-p85 binding negatively regulates PI3K activity (Fang et al. 2001); Cbl phosphorylation increased PI3K ubiquitination and proteasome degradation (Dufour et al. 2008). Cbl association with members of the Crk family is mediated by phosphorylation of Y700 and Y774 (Andoniou et al. 1996), binding with Vav is mediated by Y770 (Marengere et al 1997).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P22681-1",
"P07947-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-912629",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912629"
}
]
},
{
"id": "R-HSA-9606163",
"name": "p-SYK and LYN phosphorylate BTK",
"equation": "",
"summary": "LYN and activated (phosphorylated) SYK phosphorylate BTK (Baba et al. 2001, Lin et al. 2009, also inferred from chicken homologs and mouse homologs) after BTK is recruited to the plasma membrane by phosphorylated BLNK (Baba et al. 2001) and phosphoinositol 3,4,5-trisphosphate (PIP3) (Salim et al. 1996). Phosphorylation of tyrosine-551 occurs within 30 seconds of B cell receptor activation and returns to low phosphorylation after 30 minutes (Nisitani et al. 1999).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q06187-1",
"P07948-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-9606163",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9606163"
}
]
},
{
"id": "R-HSA-9664261",
"name": "Src phosphorylate SYK in IgG:Leishmania surface:p-FCGR3A:SYK",
"equation": "",
"summary": "Multiple sites of phosphorylation are known to exist in SYK, which both regulate its activity and also serve as docking sites for other proteins. Some of these sites include Y131 of interdomain A, Y323, Y348, and Y352 of interdomain B, and Y525 and Y526 within the activation loop of the kinase domain and Y630 in the C-terminus (Zhang et al. 2002, Lupher et al. 1998, Furlong et al. 1997). Phosphorylation of these tyrosine residues disrupts autoinhibitory interactions and results in kinase activation even in the absence of phosphorylated ITAM tyrosines (Tsang et al. 2008). SYK is primarily phosphorylated by Src family kinases and this acts as an initiating trigger by generating few molecules of activated SYK which are then involved in major SYK autophosphorylation (Hillal et al. 1997).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07947-1",
"P07948-1",
"P09769-1",
"P08631-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-9664261",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664261"
}
]
},
{
"id": "R-HSA-9664275",
"name": "Src phosphorylates CD3 dimers in IgG:Lma antigens:FCGR3A:CD3 dimers",
"equation": "",
"summary": "After cross linking, Fc gamma receptors are sequestered to lipid rafts where they are complexed with some of the tyrosine kinases of Src family and undergo phosphorylation on the tyrosine residues contained in conserved ITAM sequences. At least six out of nine members of the Src family kinases (SRC, FYN, FGR, HCK, YES and LYN ) have been identified in the phagocytic cells and are implicated in the initiation of Fc gamma mediated signaling. (Suzuki et al. 2000, Majeed et al. 2001, Kwiatkowska et al. 2003). Some of these kinases have been found associated with specific receptors. In monocytes HCK and LYN have been found associated with FCGRI (Durden et al. 1995), whereas only HCK with FCGRIIA (Ghazizadeh et al. 1994) while FGR in neutrophils (Hamada et al. 1993) and LCK in NK cells with FCGRIIIA (Pignata et al. 1993)
The implication of Src kinases in phosphorylation was first supported by pharmacological findings that herbimycin A, a tyrosine kinase inhibitor relatively specific for Src-family kinases, potently suppressed Fc receptor mediated functions (Greenberg et al. 1993, Suzuki et al. 2000). However, their particular involvement in phagocytosis remains unclear, as targeted disruption of single or multiple Src family genes did not result in significant alterations in phagocytosis (Hunter et al. 1993, Fitzer Attas et al. 2000, Suzuki et al. 2000). HCK, FGR and LYN triple-deficient (-/-) macrophages have shown significant delays in FCGR mediated phagocytosis, but these deficiencies do not completly disrupt the process (Fitzer Attas et al. 2000).
Tyrosine residues Y288 and Y304 (Y282 and Y298 according to the literature reference, it is 6 residues shorter compared to uniprot entry due to an alternate initiation codon usage), within ITAM sequence in the cytoplasmic domain of FCGRIIA are the key target sites that are phosphorylated by Src family kinases (Mitchell et al, 1994). In case of FCGRIA and FCGRIIIA the specific tyrosine residues within ITAMs of the associated gamma/zeta chains are phosphorylated by activated Src family kinases (SFKs) (Park et al. 1993).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07947-1",
"P07948-1",
"P09769-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9664275",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664275"
}
]
},
{
"id": "R-HSA-9670412",
"name": "Phosphorylation of STATs downstream of KIT mutants",
"equation": "",
"summary": "Extracellular- , juxtamembrane- and kinase-domain mutants of KIT have been shown to activate the STAT pathway, as assessed by STAT phosphorylation. The biological relevance of each STAT isoform varies between tumor types (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004; reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670412",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670412"
}
]
},
{
"id": "R-HSA-9670413",
"name": "JAK2 binds to p-KIT mutants",
"equation": "",
"summary": "Activation of STAT signaling has been observed downstream of a number of oncogenic KIT mutants, both juxtamembrane and kinase domain mutants, although the biological relevance or each STAT isoform varies between tumor types (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hana et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004). Although the pathway details haven't been examined in all cases, this likely occurs through the recruitment of JAK2 and SRC family kinases, as is the case for the wild type receptor (reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670413",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670413"
}
]
},
{
"id": "R-HSA-9670414",
"name": "KIT mutants bind SFKs",
"equation": "",
"summary": "Signaling downstream of KIT mutants occurs in part through SRC family kinases, as is the case for the wild-type receptor (Paronetto et al, 2004; Krystal et al, 1998; Schittenhelm et al, 2006; Tatton et al, 2003; Timokhina et al, 1998; reviewed in Lanneartsson and Roonstrand, 2012). The dependence of different KIT mutants on SRC family signaling varies, however, with mutants such as the common D816V showing less requirement for SFK-mediated signaling (Sun et al, 2009).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670414",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670414"
}
]
},
{
"id": "R-HSA-9670416",
"name": "Recruitment of STATs by KIT mutants",
"equation": "",
"summary": "Extracellular- , juxtamembrane- and kinase-domain mutants of KIT have been shown to signal through the STAT pathway, although the biological relevance or each STAT isoform varies between tumor types (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004). Although the pathway details haven't been examined in all cases, STAT pathway activation likely occurs through the recruitment of JAK2 and SRC family kinases, as is the case for the wild type receptor (reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670416",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670416"
}
]
},
{
"id": "R-HSA-9670417",
"name": "Dimerization of STATs downstream of KIT mutants",
"equation": "",
"summary": "Activation of STAT signaling suggests that STATs dimerize downstream of activating KIT mutations as is the case with the wild-type receptor, although this hasn't been directly demonstrated in all cases (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004; reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670417",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670417"
}
]
},
{
"id": "R-HSA-9670418",
"name": "Phosphorylation of JAK2 downstream of KIT mutants",
"equation": "",
"summary": "Although the details haven't been examined in detail in all cases, phosphorylation of JAK2 likely occurs downstream of oncogenic mutations of KIT, as is the case for the wild-type receptor (Brizzi et al, 1999; Ning et al, 2001; Hirota et al, 1998; reviewed in Lennartsson and Roonstrand, 2012).; ;",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670418",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670418"
}
]
},
{
"id": "R-HSA-9670426",
"name": "Disassociation and translocation of STATs to the nucleus downstream of KIT mutants",
"equation": "",
"summary": "STATs are assumed to dissociate from the receptor and translocate to the nucleus downstream of activated KIT receptors to propagate STAT-dependent signaling (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004; reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, nucleoplasm, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670426",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670426"
}
]
},
{
"id": "R-HSA-9674546",
"name": "CSF3 dimer:2xCSF3R:LYN:JAK1 induces phosphorylation of JAK1",
"equation": "",
"summary": "JAK1 is phosphorylated by an unknown kinase in response to CSF3 binding CSF3R (Nicholson et al. 1994, Tian et al. 1994, Marino and Roguin 2008). Phosphorylated JAK1 is required for subsequent phosphorylation of CSF3R (Shimoda et al. 1997, inferred from mouse homologs). The SRC-related protein kinase LYN is constitutively associated with CSF3R (Corey et al. 1994).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07948-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9674546",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674546"
}
]
},
{
"id": "R-HSA-9674558",
"name": "p-Y-JAK1 phosphorylates CSF3R in CSF3 dimer:2xCSF3R:LYN:p-Y-JAK1",
"equation": "",
"summary": "After JAK1 is phosphorylated and thereby activated in response to CSF3 binding CSF3R, the resulting p-Y-JAK1 phosphorylates tyrosine residues of the cytosolic domain of CSF3R (Nicholson et al. 1994, Shimoda et al. 1997, inferred from mouse homologs). The phosphorylated tyrosine residues of CSF3R then recruit effector proteins such as kinases, STATs, and RAS activators.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07948-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9674558",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674558"
}
]
},
{
"id": "R-HSA-9674562",
"name": "CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2 binds STAT1,3,5",
"equation": "",
"summary": "The STAT proteins STAT1 (Tian et al. 1994), STAT3 (Tian et al. 1994, Tian et al. 1996, Ward et al. 1999, Marino and Roguin 2008), and STAT5 (STAT5A and STAT5B) (Tian et al. 1996) bind phosphotyrosines of the cytosolic domain of CSF3R. The membrane-proximal region of the cytosolic domain of CSF3R is sufficient to activate STAT1 and STAT5. Activation of STAT3 by low concentrations of CSF3 (G-CSF) requires a membrane-distal region of CSF3R (Ward et al. 1999).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9674562",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674562"
}
]
},
{
"id": "R-HSA-9674563",
"name": "CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2:p-Y-STAT1,3,5 dissociates yielding CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2 and p-Y-STAT1,3,5",
"equation": "",
"summary": "After phosphorylation while bound to phospho-CSF3R at the plasma membrane, p-STAT1,3,5 dissociates from CSF3R prior to dimerizing and transiting to the nucleus (Tian et al. 1994, Tian et al. 1996, Ward et al. 1999, also inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9674563",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674563"
}
]
},
{
"id": "R-HSA-9674567",
"name": "p-Y-JAK1,2 phosphorylates STAT1,3,5 in CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-Y-JAK2:p-TYK2",
"equation": "",
"summary": "Phosphorylated JAK1 (p-Y-JAK1) phosphorylates the STAT proteins STAT1 (Tian et al. 1994, Tian et al. 1996, Shimoda et al. 1997, also inferred from mouse homologs), STAT3 (Tian et al. 1994, Tian et al. 1996, Shimoda et al. 1997, Ward et al. 1999, Marino and Roguin 2008, Kumar et al. 2014, also inferred from mouse homologs), and STAT5 (Tian et al. 1994, Tian et al. 1996, Shimoda et al. 1997, also inferred from mouse homologs) at the cytosolic domain of CSF3R (G-CSFR). Phosphorylated JAK2 acts redundantly with p-Y-JAK1 to phosphorylate STAT proteins (Kumar et al. 2014, also inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9674567",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674567"
}
]
},
{
"id": "R-HSA-9674808",
"name": "CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-TYK2 binds and phosphorylates SHC1, GRB2, GAB2, and PTPN11 (SHP2)",
"equation": "",
"summary": "Proteins involved in RAS-RAF-ERK signaling bind the phosphorylated cytosolic domain of CSF3R (GCSFR) and are phosphorylated (Wang et al. 2008 and inferred from mouse homologs). GRB2, GAB2, and SHC1 bind phosphorylated CSF3R directly. PTPN11 (SHP2) directly binds the phosphorylated cytosolic domain of CSF3R (inferred from mouse homologs) and also appears to bind CSF3R indirectly via phosphorylated GAB2 (inferred from mouse homologs). LYN is required for phosphorylation of GAB2 9inferred from mouse homologs). The order of binding and phosphorylation is unknown.",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-162563",
"R-HSA-508239",
"R-HSA-8983328"
],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"Q06124-2",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9674808",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674808"
}
]
},
{
"id": "R-HSA-9674816",
"name": "p-Y546,Y584-PTPN11 (in CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2:SHC:GRB2:PTPN11) dephosphorylates KRAS",
"equation": "",
"summary": "CSF3 (G-CSF) signaling activates ERKs (ERK1, ERK2) via RAS. One possible mechanism of RAS activation is the dephosphorylation of KRAS (the dominant isoform of RAS in hematopoietic cells) by phosphorylated PTPN11 (also known as SHP-2 or SHP2) (Kano et al. 2019, also inferred from dephosphorylation of the HRAS paralog in Bunda et al. 2015) bound to phosphorylated CSF3R. Dephosphorylation of RAS increases the association of RAS with its downstream effector RAF. Inhibition of PTPN11 in mouse cells indicates that this pathway accounts for most but not all activation of ERKs in response to CSF3 (Jack et al. 2009, Zhang and Friedman 2011). Guanyl nucleotide exchange factors SOS or VAV bound to GRB2 may also be responsible for some activation of RAS in response to CSF3, but this has not yet been demonstrated.",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-9674821"
],
"output_participant_list": [
"R-HSA-9674814"
],
"enzyme_list": [
"O60674-1",
"P07948-1",
"Q06124-2",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-9674816",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674816"
}
]
},
{
"id": "R-HSA-9676071",
"name": "CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1 binds and activates JAK2, TYK2, SYK, and HCK",
"equation": "",
"summary": "The kinases JAK2 (Shimoda et al. 1997, Marino and Roguin 2008), TYK2 (Shimoda et al. 1997, Marino and Roguin 2008), HCK, and SYK (Kasper et al. 1999) bind phosphorylated tyrosine residues of the cytosolic domain of CSF3R and are activated by phosphorylation (also inferred from mouse homologs). The order of their binding and the kinases responsible for their phosphorylation are incompletely characterized.",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-210620",
"R-HSA-877348",
"R-HSA-58268",
"R-HSA-167708"
],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9676071",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9676071"
}
]
},
{
"id": "R-HSA-9677579",
"name": "CSF3 dimer (GCSF dimer) binds CSF3R:JAK1:LYN",
"equation": "",
"summary": "The granulocyte colony-stimulating factor receptor (CSF3R, GCSFR, CD114) is a cell-surface receptor for the granulocyte colony-stimulating factor (CSF3, GCSF) (Fukunaga et al. 1990, Larsen et al. 1990). CSF3R is constitutively associated with the kinases LYN (Corey et al. 1994) and JAK1 (Nicholson et al. 1994) and is present on precursor cells in the bone marrow. CSF3 initiates cell proliferation and differentiation into mature neutrophilic granulocytes and macrophages.
CSF3 exists as a dimer. Only the dimer of CSF3R exhibits high affinity binding to CSF3 (Hiraoka et al. 1994). CSF3R ligand-binding causes dimerization of the receptor (Aritomi et al. 1999, Tamada et al. 2006, Layton and Hall 2006) and signal transduction through JAK-STAT, RAS-RAF-ERK1,2, and PI3K.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07948-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9677579",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9677579"
}
]
},
{
"id": "R-HSA-9677585",
"name": "CSF3 dimer:CSFR:LYN:JAK1 binds CSFR:LYN:JAK1",
"equation": "",
"summary": "Binding of the CSF3 (GCSF) dimer with the receptor CSF3R (GCSFR) causes dimerization of the receptor (Aritomi et al. 1999, Tamada et al. 2006, Layton and Hall 2006) and signal transduction through JAK-STAT, RAS-RAF-ERK1,2, and PI3K. The CSF3 receptor, CSF3R, is constitutively associated with the kinases LYN (Corey et al. 1994) and JAK1 (Nicholson et al. 1994).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07948-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9677585",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9677585"
}
]
},
{
"id": "R-HSA-9680348",
"name": "PIK3R1:PIK3CA,B,G (PI3K), PLCG2 (PLCgamma2), SHC1 (SHC), PTPN11 (SHP2), GRB2:GAB2, GRB2:GAB3, GRAP2 (MONA), CBL:GRB2, INPP5D (SHIP1), INPPL1 (SHIP2) bind PolyUb,p-8Y-CSF1R and are activated",
"equation": "",
"summary": "The PIK3R1 (p85alpha) subunit of phosphatidylinositol 3-kinase (PI3K) is phosphorylated and binds CBL and CSF1R (inferred from mouse homologs). CBL also directly binds phosphorylated CSF1R (inferred from mouse homologs). GRB2:SOS1 transiently interacts with CSF1R (inferred from mouse homologs) and PI3K (Saleem et al. 1995) in response to CSF1. SHC1 (SHC) interacts with CBL and CSF1R (inferred from mouse homologs). CBL is constitutively bound to GRB2, CBL is phosphorylated, and phosphorylated CBL binds phosphorylated SHC (inferred from mouse homologs). PLCG2 (PLC-gamma2), expressed in the myeloid lineage, binds phosphorylated tyrosine-723 of CSF1R and PLCG2 is phosphorylated in a process that requires the activity of PI3K (inferred from mouse homologs). GRAP2 (MONA) binds phosphorylated tyrosine-699 of CSF1R. GRB2 also interacts with CSF1R (Kharbanda et al. 1995) via phosphotyrosine-699 ( inferred from mouse homologs). GRAP2 binds GAB3, which is then phosphorylated (inferred from mouse homologs). In response to CSF1, the scaffolding protein GAB2 associates with INPP5D (SHIP1) and other proteins involved in CSF1 signaling and GAB2 is phosphorylated directly or indirectly by CSF1R (inferred from mouse homologs). INPPD5D also interacts with the kinase LYN (Baran et al. 2003). INPPL1 (SHIP2), a homolog of INPPD5, binds CSF1R in response to CSF1 (inferred from mouse homologs). GAB3, a homolog of GAB2, associates with CSF1R, is phosphorylated, and interacts with PI3K and PTPN11 (SHP2) (inferred from mouse homologs). The SRC family kinases SRC, FYN, and YES1 (YES) bind phosphorylated CSF1R (Courtneidge et al. 1993, Li et al. 1997, also inferred from mouse homologs). STAT proteins STAT1 and STAT3 bind CSF1R and are phosphorylated (inferred from mouse homologs). STAT5 also appears to be phosphorylated in response to CSF1 (Knowlton et al. 2010). THOC5 (FMIP) binds CSF1R and is phosphorylated (inferred from mouse homologs). The order of binding and phosphorylation of the interactors of CSF1R is unknown. Different subpopulations of CSF1R may be bound to different sets of interactors (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-197940",
"R-HSA-202367",
"R-HSA-354251",
"R-HSA-200917",
"R-HSA-9628701",
"R-HSA-373640",
"R-HSA-913354",
"R-HSA-9682751"
],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P42336-1",
"P48736-1",
"P06241-1",
"P12931-1",
"P22681-1",
"O15357-1",
"P07947-1",
"P07948-1",
"P16885-1",
"Q06124-2",
"P08631-1",
"P42338-1",
"Q92835-1"
],
"evidence": [
{
"id": "R-HSA-9680348",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680348"
}
]
},
{
"id": "R-HSA-9680388",
"name": "CSF1R-associated PLCG2 hydrolyzes phosphatidylcholine",
"equation": "",
"summary": "In response to CSF1, PLCG2 (phospholipase C gamma2) associates with CSF1R, is activated by phosphorylation, and hydrolyzes phosphatidylcholine to yield choline phosphate (ChoP, phosphocholine) and 1,2-diacylglycerol (Imamura et al. 1990, Nakamura et al. 1992, Obba et al. 2015, also inferred from mouse homologs). PLCG2 activates pathways that enhance differentiation of macrophages (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P42336-1",
"P48736-1",
"P06241-1",
"P12931-1",
"P22681-1",
"O15357-1",
"P07947-1",
"P07948-1",
"P16885-1",
"Q06124-2",
"P08631-1",
"P42338-1",
"Q92835-1"
],
"evidence": [
{
"id": "R-HSA-9680388",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680388"
}
]
},
{
"id": "R-HSA-9680389",
"name": "CSF1R-associated phosphatidylinositol 3-kinase (PI3K) phosphorylates PI(4,5)P2",
"equation": "",
"summary": "Phosphatidylinositol 3-kinase (PI3K) associated with the activated receptor for CSF1, CSF1R (M-CSFR), phosphorylates phosphatidylinositol 4,5-bisphosphate (PIP2) to yield phosphatidylinositol 3,4,5-trisphosphate (PIP3) (Saleem et al. 1995, also inferred from mouse homologs). The regulatory subunit of PI3K, PIK3R1 (p85alpha), binds phosphotyrosine-723 (721 in the mouse homologs) of CSF1R (inferred from mouse homologs). PI3K is important for proliferation, migration, and anti-inflammatory activity of macrophages (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P42336-1",
"P48736-1",
"P06241-1",
"P12931-1",
"P22681-1",
"O15357-1",
"P07947-1",
"P07948-1",
"P16885-1",
"Q06124-2",
"P08631-1",
"P42338-1",
"Q92835-1"
],
"evidence": [
{
"id": "R-HSA-9680389",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680389"
}
]
},
{
"id": "R-HSA-9705467",
"name": "SOCS1,3 binds p-4Y-CSF3R:CSF3 dimer:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2",
"equation": "",
"summary": "SOCS3 (Hortner et al. 2002) or SOCS1 binds phosphotyrosine-729 (phosphotyrosine-727 of isoform 1) of CSF3R. SOCS3 also interacts with phosphotyrosine-1007 of JAK2 (Sasaki et al. 1999). SOCS1 and especially SOCS3 inhibit the phosphorylation activity of JAK2 (van de Geijn et al. 2004).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9705467",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705467"
}
]
},
{
"id": "R-HSA-9705726",
"name": "SOCS1,3:p-4Y-CSF3R:CSF3 dimer:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2 is endocytosed",
"equation": "",
"summary": "After binding CSF3 (G-CSF), the CSF3 receptor CSF3R is internalized into endosomes (Aarts et al. 2004). Only a minor portion of CSF3R is located at the plasma membrane. Most CSF3R is located internally in the Golgi, endosomes, and lysosomes (Aarts et al. 2004). Endocytosis depends on a dileucine motif in the C-terminal region of CSF3R (inferred from mouse homologs).",
"cellular_location": "plasma membrane, endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9705726",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705726"
}
]
},
{
"id": "R-HSA-9705729",
"name": "SOCS1,3:p-4Y-CSF3R:CSF3 dimer:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2 binds CUL5, ELOB, ELOC, RNF7",
"equation": "",
"summary": "SOCS1 and SOCS3 recruit Elongin B (ELOB), Elongin C (ELOC), Cullin5 (CUL5), and RNF7 to CSF3R to form a ubiquitin E3 ligase complex (Kamura et al. 2004 and inferred from mouse homologs). SOCS3 has 100-fold higher affinity for CUL5 than SOCS1 has (inferred from mouse homologs).",
"cellular_location": "endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9705729",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705729"
}
]
},
{
"id": "R-HSA-9705738",
"name": "SOCS1,3 ubiquitinates CSF3R in SOCS1,3:p-4Y-CSF3R:CSF3 dimer:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2:CUL5:ELOB:ELOC:RNF7",
"equation": "",
"summary": "A ubiquitin E3 ligase complex assembled by SOCS3 or SOCS1 polyubiquitinates a membrane proximal lysine residue of CSF3R (K632 of the mature protein which corresponds to K655 of the preprotein) (Irandoust et al. 2007, W\u00f6lfler et al. 2009).",
"cellular_location": "endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P51668-1",
"P61077-1",
"P62837-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9705738",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705738"
}
]
},
{
"id": "R-HSA-9707977",
"name": "CSF3 dimer:2xK48polyUb-K655,p-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-Y-SYK:p-HCK:p-TYK2 translocates from the endocytic vesicle membrane to the lysosomal membrane",
"equation": "",
"summary": "Polyubiquitinated CSF3R, believed to be in a complex with with CSF3 and other signaling molecules, transits from endosomes to lysosomes (Aarts et al. 2004, Irandoust et al. 2007, W\u00f6lfler et al. 2009).",
"cellular_location": "lysosomal membrane, endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9707977",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9707977"
}
]
},
{
"id": "R-HSA-9709454",
"name": "EPOR binds EPOR agonists",
"equation": "",
"summary": "Erythropoietin (EPO) is a growth factor produced in the kidneys that stimulates the production of red blood cells. It works by promoting the division and differentiation of committed erythroid progenitors in the bone marrow. EPO binds to the erythropoietin receptor (EPOR) and triggers the JAK2/STAT5 signalling cascade which ultimately signals the activatation of nuclear target genes involved in cell division or differentiation, including the apoptosis inhibitor Bcl-x. The inhibition of apoptosis is critical in erythroid differentiation. EPO also activates other intracellular proteins involved in erythroid cell proliferation and survival.
The PEGylated functional analogue of EPO (peginesatide) and recombinant EPO forms (the epoetins) are used for the treatment of patients with anemia associated with various clinical conditions, such as chronic renal failure, antiviral drug therapy and chemotherapy (Bennet et al. 2004, Singh et al. 2006, Besarab et al. 2012, Zabaneh et al. 2015, Fishbane & Shah 2015, Zadeh 2017)",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9709454",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9709454"
}
]
},
{
"id": "R-HSA-983709",
"name": "LYN, FYN, BLK phosphorylate ITAMs of Ig-alpha (CD79A) and Ig-beta (CD79B)",
"equation": "",
"summary": "The B cell receptor (BCR) comprises an immunoglobulin complexed with a heterodimer of Ig-alpha (CD79A, MB-1) and Ig-beta (CD79B, B29). After immunoglobulin IgM or IgD binds antigen the associated Ig-alpha and Ig-beta are each observed to be phosphorylated at two tyrosine residues in the cytoplasmic immunoreceptor tyrosine-activated motif (ITAM) (Sanchez et al. 1993, Hata et al. 1994, Saouaf et al. 1994, Saouaf et al. 1995). Saouaf et al. (1995) showed that the kinase Blk could phosphorylate both tyrosines of each ITAM and that the kinase SYK specifically bound phosphorylated but not unphosphorylated ITAMs. In mouse the kinase Lyn and other kinases phosphorylate one tyrosine and Syk is believed to phosphorylate the other (Yamanashi et al. 1991, Flaswinkel and Reth 1994, Rolli et al. 2002).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07948-1",
"P51451-1",
"P29350-1"
],
"evidence": [
{
"id": "R-HSA-983709",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-983709"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-HSA-1169488",
"participant_name": "SHC1-2 [cytosol]",
"crossref": [
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{
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{
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{
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},
{
"id": "P29353",
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{
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"database": "HPA",
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{
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{
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{
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},
{
"participant_id": "R-HSA-1433505",
"participant_name": "p-Y239,Y240,Y317-SHC1-2 [cytosol]",
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{
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"url": ""
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{
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{
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{
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{
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"url": ""
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{
"id": "ENSG00000160691-SHC1",
"database": "HPA",
"url": ""
},
{
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"database": "PDB",
"url": ""
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{
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"database": "Ensembl",
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{
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"database": "PDB",
"url": ""
},
{
"id": "ENST00000448116",
"database": "Ensembl",
"url": ""
},
{
"id": "SHC1_HUMAN",
"database": "ZINC - Substances",
"url": ""
},
{
"id": "1TCE",
"database": "PDB",
"url": ""
}
]
},
{
"participant_id": "R-HSA-162563",
"participant_name": "PTPN11 [cytosol]",
"crossref": [
{
"id": "Q06124",
"database": "UniProt",
"url": ""
},
{
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"url": ""
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{
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"url": ""
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{
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"url": ""
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"url": ""
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{
"id": "ENST00000351677",
"database": "Ensembl",
"url": ""
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{
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"database": "Ensembl",
"url": ""
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{
"id": "ENSP00000340944",
"database": "Ensembl",
"url": ""
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{
"id": "ENST00000635625",
"database": "Ensembl",
"url": ""
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{
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"database": "PDB",
"url": ""
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{
"id": "7R7D",
"database": "PDB",
"url": ""
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{
"id": "7R75",
"database": "PDB",
"url": ""
},
{
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"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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