Tetraspanin-15 (TSPAN15)

Tetraspanin-15 (TSPAN15) is a cell-surface protein belonging to the tetraspanin family, characterized by four transmembrane domains, and is a key regulatory subunit of the metalloprotease ADAM10[6][1]. TSPAN15 forms heteromeric complexes with ADAM10, facilitating its exit from the endoplasmic reticulum, trafficking to the cell surface, and defining its substrate specificity[3][1][5]. The TSPAN15–ADAM10 complex acts as a functional "molecular scissor" involved in the proteolytic cleavage of key substrates such as N-cadherin, Notch, and amyloid precursor protein[1][5]. TSPAN15-mediated ADAM10 function is essential in multiple biological processes including cell adhesion, proliferation, migration, and signal transduction[2][6]. TSPAN15 is upregulated in several cancers, where it acts as a marker of poor prognosis and may contribute to tumor progression[1]. Although direct therapeutic targeting has not advanced to clinical-stage drugs, function-blocking monoclonal antibodies to TSPAN15 have been shown experimentally to impair its complex with ADAM10[1].

Other names

Tetraspanin-15TSPAN15NET7TM4SF15UNQ677/PRO1311Tspan-15NET-7Tetraspan NET-7Transmembrane 4 superfamily member 152700063A19Riktetraspan NET-7transmembrane 4 superfamily member tetraspan NET-7

Monoclonal antibodies impairing function of the ADAM10/TSPAN15 complex through direct inhibition[1]