Integrin beta-8 (ITGB8)

Integrin beta-8 is a single-pass type I transmembrane protein encoded by the ITGB8 gene in humans. It belongs to the integrin β chain family and forms heterodimeric complexes—most notably with integrin αv—to produce the αvβ8 integrin receptor. This receptor mediates cell-cell and cell-extracellular matrix interactions, especially by binding to ligands containing R-G-D sequences such as fibronectin[6]. Unusually among integrins, β8 forms an extended-closed conformation and lacks conserved cytoplasmic motifs for canonical inside-out signaling, indicating distinct regulatory mechanisms[2][3]. The αvβ8 complex uniquely activates latent TGF-β, influencing important processes in epithelial homeostasis, angiogenesis, and tumor development[3][4]. In cancer, particularly glioblastoma, integrin beta-8 modulates the balance between invasiveness and angiogenesis, and interacts with signaling molecules such as RhoGDI1 and PTP-PEST to regulate cell motility and invasion[1][3]. It is considered a relevant therapeutic target in several diseases involving abnormal angiogenesis, invasion, or inflammation[4].

Other names

Integrin β8ITGB8β8 integrinIntegrin beta chain beta 8

Inhibition of ligand binding (notably to TGF-β proforms or fibronectin); Modulation of integrin signaling and downstream pathways