Integrin alpha 5 beta 1

Integrin alpha 5 beta 1 is the principal fibronectin receptor, an RGD-dependent heterodimer assembled from CD49e and CD29. It binds fibrillar fibronectin and drives fibrillogenesis, organizing the extracellular matrix during embryogenesis, angiogenesis and wound healing; knockout of either subunit in mice is embryonic lethal with severe vascular and mesodermal defects. On tumor endothelium the heterodimer is markedly upregulated, which has motivated anti-angiogenic strategies such as volociximab and fibronectin-targeted drug delivery. Alpha 5 beta 1 also transduces outside-in signals through FAK and Src that govern cell survival and migration. Compared with alpha V beta 3, it shows higher selectivity for fibronectin over vitronectin, making it the reference receptor for fibronectin-based adhesion assays.