Abstract
Integrin beta 3 is seen as a key anti-angiogenic target for cancer treatment due to its expression on neovasculature, but the role it plays in the process is complex; whether it is pro-or anti-angiogenic depends on the context in which it is expressed. To understand precisely beta 3's role in regulating integrin adhesion complexes in endothelial cells, we characterised, by mass spectrometry, the beta 3-dependent adhesome. We show that depletion of beta 3-integrin in this cell type leads to changes in microtubule behaviour that control cell migration. beta 3-integrin regulates microtubule stability in endothelial cells through Rcc2/Anxa2-driven control of active Rac1 localisation. Our findings reveal that angiogenic processes, both in vitro and in vivo, are more sensitive to microtubule targeting agents when beta 3-integrin levels are reduced.