Integrin subunit beta-4 (ITGB4)

Integrin subunit beta-4 (ITGB4; CD104) is a transmembrane glycoprotein receptor that forms a heterodimer with integrin alpha-6, together functioning as a receptor for laminins in the extracellular matrix[2][4][7]. ITGB4 is distinguished by its unusually large cytoplasmic domain, which is critical for linking the α6β4 integrin complex to cytoskeletal structures known as hemidesmosomes—specialized adhesion structures anchoring epithelial cells to the basement membrane[1][3][5]. This integrin plays a vital role in cell adhesion, maintenance of epithelial tissue integrity, and transduction of signals that regulate cell growth, polarity, and survival[3][4][5]. Mutations in ITGB4 disrupt these functions, leading to conditions such as epidermolysis bullosa with pyloric atresia, characterized by severe skin blistering and gastrointestinal manifestations[3][4]. In cancer, altered expression and signaling through α6β4 integrin are implicated in carcinoma progression, tumor invasion, and resistance to apoptosis, making it a biomarker and research target in oncology[4][2][7].

Other names

Integrin beta-4CD104Integrin, beta 4ITGB4

Inhibition or modulation of integrin-mediated cell adhesion and migration (proposed/experimental); Disruption of α6β4 integrin interaction with extracellular matrix (proposed/experimental)