Autocatalytic phosphorylation of FGFR1c

Stable Identifier
Reaction [transition]
Homo sapiens
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Studies have mapped 8 tyrosine residues in the cytoplasmic domain of FGFR1 that are important for signaling. Autophosphorylation of residues 653 and 654, located in the activation loop of the kinase, is necessary to maintain the receptor in the active state. Phosphorylation of other tyrosine residues by the intrinsic protein tyrosine kinase activity of the activated receptor creates binding sites on its cytoplasmic tail for membrane bound docking proteins to gather intracellular signaling mediators.
Literature References
PubMed ID Title Journal Year
8622701 Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction

Burgess, WH, Jaye, M, Schlessinger, J, Sorokin, A, Dikic, I, Mohammadi, M

Mol Cell Biol 1996
16507368 Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction

Schlessinger, J, Furdui, CM, Anderson, KS, Lew, ED

Mol Cell 2006
1379698 Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis

Dionne, CA, Jaye, M, Li, N, Schlessinger, J, Honegger, AM, Mohammadi, M, Spivak, T, Li, W

Nature 1992
9139660 Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors

Hubbard, SR, Schlessinger, J, Yeh, BK, Mohammadi, M, Tang, C, Sun, L, McMahon, G, Hirth, P

Science 1997
11294897 Identification of tyrosine residues in constitutively activated fibroblast growth factor receptor 3 involved in mitogenesis, Stat activation, and phosphatidylinositol 3-kinase activation

Donoghue, DJ, Hart, KC, Robertson, SC

Mol Biol Cell 2001
Catalyst Activity

protein tyrosine kinase activity of FGFR1c homodimer bound to FGF [plasma membrane]

Orthologous Events
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