![]() To deal with these complex and error-prone processes, the ER has evolved a system centered around the calnexin family of molecular chaperones calnexins promotes the proper folding and assembly of newly synthesized glycoproteins. G protein-coupled receptors are synthesized on membrane-bound ribosomes and undergo translocation, modification, folding, oligomeric assembly, and quality control in the endoplasmic reticulum (ER). These results illustrate a critical role for calnexin in Rh1 maturation and Ca 2+ regulation and provide genetic evidence that defects in calnexin lead to retinal degeneration (Rosenbaum, 2006). Finally, mutations in calnexin lead to retinal degeneration this degeneration is enhanced by light, suggesting that calnexin's function as a Ca 2+ buffer is important for photoreceptor cell survival. Mutations in calnexin also impair the ability of photoreceptor cells to control cytosolic Ca 2+ levels following activation of the light-sensitive TRP channels. Mutations in Drosophila calnexin lead to severe defects in rhodopsin (Rh1) expression, whereas other photoreceptor cell proteins are expressed normally. A multifunctional role for calnexin has been demonstrated as both a molecular chaperone uniquely required for rhodopsin maturation and a regulator of Ca 2+ that enters photoreceptor cells during light stimulation. In sensory neurons, successful maturation of signaling molecules and regulation of Ca 2+ are essential for cell function and survival. ![]() Keywords - eye, Rhodopsin 1 (NinaE), protein folding, calcium ion binding, axon guidance, visual signal transductionĬlassification - Calreticulin/calnexin type lectin domainĬellular location - endoplasmic reticulum transmembrane protein ![]()
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