Integrin alphaVbeta3 binds p-6Y-VEGFR2

Stable Identifier
Reaction [binding]
Homo sapiens
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Several receptor tyrosine kinases (RTKs) are known to associate with integrins, and it has been suggested that focal adhesion kinase (FAK) is at the crossroads of these signaling pathways. On endothelial cells integrin alphaVbeta3 acts as a regulator of VEGFR2 signaling and shown to be necessary for angiogenic response (Hood et al. 2003). In mouse endothelial cells VEGF stimulated complex formation between VEGFR2 and beta3 integrin. This association between alphaVbeta3 with VEGFR2 appears to be synergistic, because VEGFR2 activation induces beta3 integrin tyrosine phosphorylation, which, in turn, enhances the phosphorylation of VEGFR2 and mediates the activation of mitogenic pathways involving focal adhesion kinase (FAK) and stress-activated protein kinase-2/p38 (SAPK2/p38) (Masson-Gadais et al. 2003, Mahabaleshwar et al. 2006, Somanath et al. 2009). This promotes activation of alphaVbeta3 and results in the increase of ligand binding ability (integrin activation), integrin ligation, and phosphorylation of beta3 integrin by cSrc.
Literature References
PubMed ID Title Journal Year
19267251 Cooperation between integrin alphavbeta3 and VEGFR2 in angiogenesis

Somanath, PR, Byzova, TV, Malinin, NL

Angiogenesis 2009
17030947 Integrin signaling is critical for pathological angiogenesis

Byzova, TV, Mahabeleshwar, GH, Feng, W, Phillips, DR

J. Exp. Med. 2006
12820653 Integrin alphavbeta3, requirement for VEGFR2-mediated activation of SAPK2/p38 and for Hsp90-dependent phosphorylation of focal adhesion kinase in endothelial cells activated by VEGF

Masson-Gadais, B, Houle, F, Huot, J, Laferrière, J

Cell Stress Chaperones 2003
Orthologous Events
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