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, PPTN11/SHP2 phosphorylation, and activation of MAPK, PI3K and STAT pathways. These studies also identified a role for the PLCG1-binding tyrosine residue, Y760, in STAT activation, and a potential role for tyrosine 770 as a negative regulator of FGFR3 signaling.
Burgess, WH, Jaye, M, Schlessinger, J, Sorokin, A, Dikic, I, Mohammadi, M
Dionne, CA, Jaye, M, Li, N, Schlessinger, J, Honegger, AM, Mohammadi, M, Spivak, T, Li, W
Bellot, F, Dionne, CA, Jaye, M, Schlessinger, J, Rotin, D, Honegger, AM, Rubinstein, M, Mohammadi, M, Fischer, R, Li, W
Donoghue, DJ, Hart, KC, Robertson, SC
protein tyrosine kinase activity of FGFR3b homodimer bound to FGF [plasma membrane]
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