Reactome | Autocatalytic phosphorylation of FGFR2c

Autocatalytic phosphorylation of FGFR2c

Stable Identifier

R-HSA-190413

Type

Reaction [transition]

Species

Homo sapiens

Compartment

plasma membrane, cytosol, extracellular region

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

Signal Transduction (Homo sapiens)

- Signaling by Receptor Tyrosine Kinases (Homo sapiens)
  - Signaling by FGFR (Homo sapiens)
    - Signaling by FGFR2 (Homo sapiens)
      - FGFR2 ligand binding and activation (Homo sapiens)
        
        FGFR2c ligand binding and activation (Homo sapiens)
        
        Autocatalytic phosphorylation of FGFR2c (Homo sapiens)

General

SBML | | PDF

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 the activated FGFR2c receptor leads to multiple phosphorylation events, creating a number of binding sites on its cytoplasmic tail for membrane bound docking proteins to gather intracellular signaling mediators. Two isoforms of FGFR2c generated by alternative splicing and differing only by the presence ("long") or absence ("short") of two amino acid residues at positions 428-429 are equally active in autophosphorylation, but differ in their abilities to interact with downstream targets. Based on sequence alignment, FGFR2 contains all 8 of the 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 Mohammadi, M, Dikic, I, Sorokin, A, Burgess, WH, Jaye, M, Schlessinger, J	Mol Cell Biol	1996
1697263	Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors Dionne, CA, Crumley, G, Bellot, F, Kaplow, JM, Searfoss, G, Ruta, M, Burgess, WH, Jaye, M, Schlessinger, J	EMBO J	1990
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