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.