Integrin alpha-6 beta-4 (α6β4 integrin)

Integrin alpha-6 beta-4 is a heterodimeric cell-surface receptor composed of alpha-6 (CD49f, encoded by ITGA6) and beta-4 (CD104, encoded by ITGB4) subunits[1][2]. It is a key component of hemidesmosomes—structures that anchor epithelial cells to the basement membrane through binding to laminins in the extracellular matrix[3][5][6]. The beta-4 subunit has a remarkably large cytoplasmic domain, which connects to cytoskeletal proteins such as plectin, facilitating stable epithelial adhesion and contributing to tissue integrity[2][4]. Integrin α6β4 also participates in intracellular signaling, impacting pathways that regulate cell migration, proliferation, and survival. Its dysregulation—such as overexpression or altered function—is frequently associated with increased cell motility and invasion in carcinomas, highlighting its importance in cancer progression, and is under study as a therapeutic and prognostic target[3][7]. In normal physiology, integrin α6β4 is essential for epithelial tissue maintenance, but its disruption can lead to diseases involving loss of tissue cohesion, such as certain blistering skin disorders and colitis[1][3][5].

Other names

Integrin α6β4ITGA6-ITGB4CD49f/CD104Laminin receptorTSP180 (historical, less common)

Blocking integrin-laminin interaction to inhibit cell adhesion or migration; Modulating signaling pathways (e.g., inhibition of PI3K or RhoA activation triggered by this integrin)