Autocatalytic phosphorylation of FGFR1b

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
1656221 A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1

Bellot, F, Dionne, CA, Jaye, M, Schlessinger, J, Rotin, D, Honegger, AM, Rubinstein, M, Mohammadi, M, Fischer, R, Li, W

Mol Cell Biol 1991
Catalyst Activity

protein tyrosine kinase activity of FGFR1b homodimer bound to FGF [plasma membrane]

Orthologous Events
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