Autocatalytic phosphorylation of FGFR4

Stable Identifier
R-HSA-190326
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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The intrinsic protein tyrosine kinase activity of activated FGF receptor 4 catalyzes multiple phosphorylation events, creating a number of binding sites for membrane bound docking proteins to gather intracellular signaling mediators. Based on sequence alignment, FGFR4 contains 5 of the 8 cytoplasmic tyrosine residues identified in FGFR1.

Literature References
PubMed ID Title Journal Year
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
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
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
11294897 Identification of tyrosine residues in constitutively activated fibroblast growth factor receptor 3 involved in mitogenesis, Stat activation, and phosphatidylinositol 3-kinase activation

Hart, KC, Robertson, SC, Donoghue, DJ

Mol Biol Cell 2001
Participants
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Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of FGFR4 homodimer bound to FGF [plasma membrane]
Physical Entity
Activity
Orthologous Events
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Created