Calnexin, calreticulin and the folding of glycoproteins

Trends Cell Biol. 1997 May;7(5):193-200. doi: 10.1016/S0962-8924(97)01032-5.

Abstract

Calnexin and calreticulin are molecular chaperones in the endoplasmic reticulum (ERJ. They are lectins that interact with newly synthesized glycoproteins that have undergone partial trimming of their core N-linked oligosaccharides. Together with the enzymes responsible for glucose removal and a glucosyltransferase that re-glucosylates already-trimmed glycoproteins, they provide a novel mechanism for promoting folding, oligomeric assembly and quality control in the ER.