alpha5beta1
Alpha5beta1, commonly written as integrin α5β1, is a heterodimeric cell-surface receptor in the integrin family. It is formed by the pairing of ITGA5 (alpha-5) and ITGB1 (beta-1) subunits and is frequently referred to as VLA-5. The receptor is broadly expressed, especially on endothelial cells and fibroblasts, where it mediates adhesion to extracellular matrix components, with a primary affinity for fibronectin.
Ligand recognition and activation are centered on fibronectin. α5β1 binds the RGD motif within fibronectin, with
Signaling pathways downstream of α5β1 include focal adhesion kinase (FAK), Src family kinases, and the PI3K-Akt
Clinical and research relevance: due to its involvement in angiogenesis and metastasis, α5β1 has been explored
---