CD42c/GP-Ib beta

Glycoprotein Ib beta (CD42c) is the small transmembrane subunit that anchors the vWF-binding module of GPIb alpha to the platelet cytoskeleton. Through its cytoplasmic tail, GP-Ib beta binds filamin A, physically connecting the GPIb-IX-V complex to the actin network and translating ligand capture into intracellular signaling. Together with GPIb alpha it participates in the Src-dependent pathways that amplify platelet activation downstream of vWF tethering. Inherited GP1BB mutations reproduce Bernard-Soulier syndrome, often with cytoplasmic-tail truncations that uncouple the receptor from filamin, and anti-CD42c antibodies have been reported in immune thrombocytopenia. The subunit illustrates how a ligand-free chain still dictates complex function.