PLCG1 disassociates from VEGFR2 and translocate to PM

Stable Identifier
R-HSA-4420202
Type
Reaction [dissociation]
Species
Homo sapiens
Compartment
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Following tyrosine phosphorylation and activation, PLCG1 dissociates from the VEGFR2 receptor and associates with its substrate phosphatidylinositol (4,5)-bisphosphate (PIP2) in the plasma membrane. PLCG1 hydrolyses PIP2 resulting in the generation of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG is an activator of PKC which leads to subsequent activation of MAP kinase, resulting in increased endothelial cell proliferation. IP3 acts upon receptors in the endoplasmic reticulum causing release of intracellular calcium. Elevation of cytosolic Ca2+ stimulates eNOS to produce nitric oxide (NO) causing vascular dilation. Entry of extracellular calcium through specific channels is important for the activation of certain proteins (Takahashi et al. 2001, Takahashi et al. 1999, Xia et al. 1996).

Literature References
PubMed ID Title Journal Year
11600407 Role of PLCgamma and Ca(2+) in VEGF- and FGF-induced choroidal endothelial cell proliferation

McLaughlin, AP, De Vries, GW

Am. J. Physiol., Cell Physiol. 2001
11387210 A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells

Takahashi, T, Yamaguchi, S, Chida, K, Shibuya, M

EMBO J 2001
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