Interleukin-17 receptor C (IL-17RC)

Interleukin– 7 receptor C is a type I transmembrane glycoprotein that forms part of the heteromeric interleukin– 7 receptor complex together with interleukin– 7RA. It binds pro-inflammatory cytokines including interleukin– 7A, interleukin– F, and their heterodimers. The canonical human protein consists of an extracellular domain with two fibronectin-type III domains responsible for ligand binding; a single-pass transmembrane region; and an intracellular SEFIR domain involved in signal transduction. Expression is highest in nonhematopoietic tissues such as prostate, liver, kidney, thyroid gland, and joints but low in hematopoietic cells[7]. Upon ligand engagement—either alone or together with other subunits—it mediates activation of downstream pathways leading to production of chemokines that recruit neutrophils and promote inflammation. Dysregulation or overactivation contributes to pathogenesis in several autoimmune disorders including psoriasis and rheumatoid arthritis. Structural studies reveal it can form complexes not only with its canonical partner but also independently mediate signaling under certain conditions—a property relevant for drug development targeting this axis[5].

Other names

Interleukin-17 γ receptorIL17RCIl17rl (in some species)

Drugs targeting this pathway generally act as antagonists to block ligand-receptor interaction—most commonly by neutralizing the cytokines (e.g., anti–IL‑17A antibodies) rather than directly binding to the receptor subunits themselves. A soluble version of IL‑17RC has been proposed as an antagonist for both IL‑17A and IL‑17F signaling.