Bergeron J J, Brenner M B, Thomas D Y, Williams D B
Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.
Trends Biochem Sci. 1994 Mar;19(3):124-8. doi: 10.1016/0968-0004(94)90205-4.
Calnexin is a new type of molecular chaperone that interacts with many nascent membrane and soluble proteins of the secretory pathway. Calnexin is unrelated to molecular chaperones of the Hsp60, Hsp70 and Hsp90 families, and is further distinguished from them in that it is an integral membrane protein. One of its demonstrated functions is the retention of incorrectly or incompletely folded proteins, suggesting that calnexin is a component of the quality control system of the endoplasmic reticulum.
钙连接蛋白是一种新型分子伴侣,它与分泌途径中的许多新生膜蛋白和可溶性蛋白相互作用。钙连接蛋白与热休克蛋白60、热休克蛋白70和热休克蛋白90家族的分子伴侣无关,并且与它们的进一步区别在于它是一种整合膜蛋白。其已被证实的功能之一是保留错误折叠或未完全折叠的蛋白质,这表明钙连接蛋白是内质网质量控制系统的一个组成部分。