Phospholipase C-mediated cascade; FGFR2

Stable Identifier
R-HSA-5654221
Type
Pathway
Species
Homo sapiens
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ReviewStatus
5/5
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Phospholipase C-gamma (PLC-gamma) is a substrate of the fibroblast growth factor receptor (FGFR) and other receptors with tyrosine kinase activity. It is known that the src homology region 2 (SH2 domain) of PLC-gamma and of other signaling molecules (such as GTPase-activating protein and phosphatidylinositol 3-kinase-associated p85) direct their binding toward autophosphorylated tyrosine residues of the FGFR. Recruitment of PLC-gamma results in its phosphorylation and activation by the receptor. Activated PLC-gamma hydrolyzes phosphatidyl inositol[4,5] P2 to form the second messengers diacylglycerol (DAG) and Ins [1,4,5]P3, which stimulate calcium release and activation of calcium/calmodulin dependent kinases.
Literature References
PubMed ID Title Journal Year
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
15863030 Cellular signaling by fibroblast growth factor receptors

Schlessinger, J, Eswarakumar, VP, Lax, I

Cytokine Growth Factor Rev 2005
10579907 Phospholipase C-gamma as a signal-transducing element

Ji, Q, Carpenter, G

Exp Cell Res 1999
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