Transforming growth factor beta receptor 3 (TGFBR3) (TGFBR3)

Transforming growth factor beta receptor 3 (TGFBR3), commonly known as Betaglycan, is a membrane-bound proteoglycan that functions as a critical co-receptor for the TGF-beta superfamily (UniProt P59895). The Zona Pellucida (ZP) domain is a highly conserved structural motif located in the C-terminal region of its extracellular domain, which is essential for the high-affinity binding of ligands such as TGF-beta 2 and Inhibin A (Lin et al., 2006). Unlike the type I and II TGF-beta receptors, TGFBR3 lacks an intracellular signaling kinase domain and instead regulates signaling by presenting ligands to signaling receptors or by being shed as a soluble form (sTGFBR3) that acts as a decoy (Bernabeu et al., 2009). In many human cancers, including breast, lung, and prostate cancer, TGFBR3 expression is frequently lost, which correlates with increased cell motility, invasion, and metastasis, establishing its role as a potent tumor suppressor (Gatza et al., 2010). Therapeutic strategies targeting this molecule often focus on utilizing the soluble extracellular domain to sequester pathological TGF-beta ligands in fibrotic and malignant conditions (Bilandzic et al., 2009). Additionally, the ZP domain specifically mediates interactions with inhibins, making it a target of interest in reproductive cancers and endocrine disorders.

Other names

BetaglycanTGF-beta receptor type IIIBGCANTransforming growth factor beta receptor IIITGFR-3

Acts as a co-receptor that presents ligands to signaling receptors or functions as a decoy receptor to sequester ligands when shed from the cell surface.