Reactome | Autocatalytic phosphorylation of FGFR3c

Autocatalytic phosphorylation of FGFR3c

Stable Identifier

R-HSA-190388

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, cytosol, extracellular region

ReviewStatus

5/5

Locations in the PathwayBrowser

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Signal Transduction (Homo sapiens)

- Signaling by Receptor Tyrosine Kinases (Homo sapiens)
  - Signaling by FGFR (Homo sapiens)
    - Signaling by FGFR3 (Homo sapiens)
      - FGFR3 ligand binding and activation (Homo sapiens)
        
        FGFR3c ligand binding and activation (Homo sapiens)
        
        Autocatalytic phosphorylation of FGFR3c (Homo sapiens)

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The intrinsic protein tyrosine kinase activity of activated FGF receptor 3 catalyzes multiple phosphorylation events, creating a number of binding sites on its cytoplasmic tail for membrane bound docking proteins to gather intracellular signaling mediators. Based on sequence alignment, FGFR3 contains 6 of the 8 cytoplasmic tyrosine residues identified in FGFR1. Mutagenesis studies highlight the importance of tyrosine residue 724 in signaling mediated by FGFR3, including transformation, PPTN11/SHP2 phosphorylation, and activation of MAPK, PI3K and STAT pathways. These studies also identified a role for the PLCG1-binding tyrosine residue, Y760, in STAT activation, and a potential role for tyrosine 770 as a negative regulator of FGFR3 signaling.

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 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
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