Overview:

Kinase insert domain receptor (KDR or VEGFR) is a growth factor receptor tyrosine kinase that plays a pivotal role in endothelial cell proliferation and differentiation. KDR binds VEGF with high affinity and this interaction is implicated in angiogenesis (1). The expression levels of VEGF and KDR are highly correlated during the normal development of the ocular vasculature in humans (1). Induction of angiogenesis is a critical step in tumor progression, and inhibitors of KDR have been demonstrated both to promote tumor regression and reduce metastatic potential in preclinical studies (2). Autophosphorylation of KDR occurs at Tyr951, Tyr996, Tyr1054 and Tyr1059 and phosphorylation at Tyr1214 is associated with interactions with downstream effector molecules (3).

References:

1. Neufeld, G. et al: Vascular endothelial growth factor (VEGF) and its receptors. FASEB J. 1999 Jan;13(1):9-22. 2. Zhu, Z. et al: Inhibition of tumor growth and metastasis by targeting tumor-associated angiogenesis with antagonists to the receptors of vascular endothelial growth factor. Invest New Drugs. 1999;17(3):195-212.3. Lamalice L. et al: Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF. J Biol Chem. 2006 Nov 10;281(45):34009-20.