Integrin beta-6 subunit (ITGB6)

Integrin beta-6 subunit (ITGB6) is a type I transmembrane glycoprotein that dimerizes exclusively with the αv subunit to form the integrin αvβ6, a cell surface receptor found primarily on epithelial cells[1][5][6]. As part of the integrin superfamily, αvβ6 mediates cell adhesion by binding extracellular matrix proteins containing the Arg-Gly-Asp (RGD) motif, such as fibronectin, cytotactin, and latent TGF-β1[1][3][6]. αvβ6 is minimally expressed in most adult tissues under basal conditions but is strongly upregulated during tissue remodeling, wound healing, cancer progression, and fibrotic responses[1][2]. Its activation of latent TGF-β1 is a key mechanism driving epithelial–mesenchymal transition, fibrosis, immunosuppression, and tumor invasion[1][2][6]. αvβ6 is an emerging therapeutic target and biomarker in oncology and fibrotic diseases, and several drugs and imaging agents targeting this molecule are in preclinical or clinical development[2].

Other names

Integrin beta chain beta-6Integrin beta-6ITGB6CD105 (less common)β6 integrin subunitIntegrin β6

Blockade of integrin αvβ6 disrupts TGF-β1 activation and epithelial-matrix signaling, leading to reduced cell proliferation, invasion, fibrosis, and immune suppression[2]. Antagonistic antibodies can elicit anti-tumor immune responses, synergizing with immune checkpoint blockade[2].