Autocatalytic phosphorylation of FGFR1b

Stable Identifier
R-HSA-190427
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
16507368 Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction

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

Mol Cell 2006
8622701 Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction

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

Mol Cell Biol 1996
1379698 Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis

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

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

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

Mol Cell Biol 1991
Participants
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Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of FGFR1b homodimer bound to FGF [plasma membrane]
Physical Entity
Activity
Orthologous Events
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