Integrin alpha V beta 1 (αVβ1) is a widely expressed adhesion receptor formed by the non-covalent association of the αV and β1 (CD29) subunits. Its activity is regulated by a conformational shift from a folded, low-affinity state to an extended, high-affinity state, a process triggered by divalent cations and intracellular signaling. As a canonical RGD-binding integrin, it interacts with ligands including vitronectin, fibronectin, and osteopontin. This interaction is central to its role in mediating cell migration, where its modest binding affinity enables the cyclic attachment and detachment necessary for cell movement. Furthermore, αVβ1 is implicated in cellular differentiation and is co-opted by pathogens, such as foot-and-mouth disease virus, for host cell entry.