Reaction: CSF1R trans-autophosphorylates on multiple tyrosine and serine residues
- in pathway: Signaling by CSF1 (M-CSF) in myeloid cells
Following dimerization of the CSF-1 receptor (CSF1R), it undergoes trans-autophosphorylation on multiple tyrosine residues by its intrinsic kinase activity (Rohrschneider et al. 1997, Chihara et al. 2010). Tyrosine-561 (tyrosine-559 in the mouse homolog) in the juxtamembrane domain inhibits the kinase activity of CSF1R and is phosphorylated first, thus activating the kinase activity of CSF1R (inferred from the mouse homolog). Other tyrosine residues that are autophosphorylated are tyrosine-546 in the juxtamembrane domain, tyrosines-699,708,723 in the kinase insert domain, tyrosine-809 in the kinase domain, and tyrosines-923,969 in the C-terminal domain (Chihara et al. 2010, reviewed in Hamilton 1997, and inferred from the mouse homolog).
Reaction - small molecule participants:
ADP [cytosol]
ATP [cytosol]
Reactome.org reaction link: R-HSA-389159
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Reaction input - small molecules:
ATP(4-)
Reaction output - small molecules:
ADP(3-)
Reactome.org link: R-HSA-389159