Retinoschisin Protein (RS1)

Retinoschisin (RS1) is a soluble, cell-surface lectin crucial for retinal structure and function. Encoded by the RS1 gene on chromosome Xp22.13, it is specifically expressed in photoreceptor and bipolar cells of the retina, as well as pinealocytes. The protein contains a discoidin domain and forms oligomeric structures (homo16mer) that facilitate strong membrane adhesion between retinal cells. RS1 acts as an extracellular cell adhesion molecule, binding to plasma membranes of photoreceptors and bipolar cells and interacts with Na/K ATPase complexes (α3/β2 isoforms). Mutations in RS1 cause X-linked juvenile retinoschisis, leading to retinal splitting and progressive vision loss. Key interacting partners include Na/K ATPase and SARM1, which are important for maintaining retinal tissue integrity and regulating intracellular signaling.

Other names

X-linked juvenile retinoschisis proteinXLRS1XLRS1_HUMAN

Currently, no drugs directly target RS1. Gene therapy approaches are under investigation.