Autocatalytic phosphorylation of FGFR4

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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
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
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
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 FGFR4 homodimer bound to FGF [plasma membrane]

Orthologous Events
Cite Us!