Reactome | CSF1R trans-autophosphorylates on multiple tyrosine and serine residues

CSF1R trans-autophosphorylates on multiple tyrosine and serine residues

Stable Identifier

R-HSA-389159

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane

ReviewStatus

5/5

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CSF1R trans-autophosphorylates on multiple tyrosine and serine residues

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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).

Literature References

PubMed ID	Title	Journal	Year
20489731	IL-34 and M-CSF share the receptor Fms but are not identical in biological activity and signal activation Chihara, T, Suzu, S, Hassan, R, Chutiwitoonchai, N, Hiyoshi, M, Motoyoshi, K, Kimura, F, Okada, S	Cell Death Differ.	2010
8981370	Growth and differentiation signals regulated by the M-CSF receptor Rohrschneider, LR, Bourette, RP, Lioubin, MN, Algate, PA, Myles, GM, Carlberg, K	Mol Reprod Dev	1997