Source:http://www.reactome.org/biopax/48887BiochemicalReaction1761
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Authored: de Bono, B, 2007-01-10 10:27:18,
Reviewed: Mohammadi, M, 2007-02-06 21:44:35,
The intrinsic protein tyrosine kinase activity of activated FGF receptor 3 catalyzes multiple phosphorylation events, creating a number of binding sites on its cytoplasmic tail for membrane bound docking proteins to gather intracellular signaling mediators. Based on sequence alignment, FGFR3 contains 6 of the 8 cytoplasmic tyrosine residues identified in FGFR1. Mutagenesis studies highlight the importance of tyrosine residue 724 in signaling mediated by FGFR3, including transformation, SHP2 phosphorylation, and activation of MAPK, PI3K and STAT pathways. These studies also identified a role for the PLCgamma-binding tyrosine residue, Y760, in STAT activation, and a potential role for tyrosine 770 as a negative regulator of FGFR3 signaling.
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Autocatalytic phosphorylation of FGFR3c
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2.7.10
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