Lectins as chaperones in glycoprotein folding

Abstract

N-glycosylation allows newly synthesized glycoproteins to interact with a lectin-based chaperone system in the endoplasmic reticulum. Binding to the lectins calnexin and calreticulin is mediated by monoglucosylated oligosaccharides that are produced transiently by the deglucosylation and reglucosylation of substrate glycoproteins during their maturation process. In mammalian cells, calnexin, calreticulin and associated factors promote the correct folding and oligomerization of many glycoproteins, providing unique quality control and chaperone functions specific for glycoproteins in the endoplasmic reticulum.