Plexin C1 (PlexinC1)

Plexin C1 is a cell-surface receptor prominently expressed in the nervous, immune, and cardiovascular systems, where it functions in repulsive signal transduction by binding ligands such as semaphorin 7A and certain viral proteins (e.g., A39R)[1][2]. It features a unique extracellular domain structure with two PSI and four IPT domains, and the semaphorin-binding Sema domain, distinguishing it from other plexins[2]. Upon ligand binding, Plexin C1 dimerizes, enabling activation of its intracellular GAP activity and downstream signaling pathways responsible for cell migration, immune regulation, and axon guidance[1][2]. This receptor's structure-function relationship is particularly relevant for disease processes involving cell migration, immune modulation, and viral pathogenesis, making it an emerging therapeutic target, though drug development is still in preliminary stages.

Other names

Plexin-C1PLXNC1VESPRVESPR-1

Competitive inhibition or modulation of semaphorin binding; Dimerization-dependent activation leading to intracellular signaling changes; Viral mimicry (by viral proteins such as A39R which structurally resembles endogenous ligand and activates or blocks PlexinC1 signaling).