Lectins as chaperones in glycoprotein folding.
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.
Trombetta
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Department of Cell Biology, Yale Medical School, New Haven, CT 06520-8002, USA. sergio.trombetta@yale.edu
Helenius
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D000818:Animals; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D037281:Calnexin; D037282:Calreticulin; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry* / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D007535:Isomerases / Q000378:metabolism; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D019704:Protein Disulfide-Isomerases; D017510:Protein Folding; D012261:Ribonucleoproteins / Q000378:metabolism*
D002135:Calcium-Binding Proteins; D037282:Calreticulin; D006023:Glycoproteins; D006360:Heat-Shock Proteins; D037102:Lectins; D012261:Ribonucleoproteins; D037281:Calnexin; D007535:Isomerases; D019704:Protein Disulfide-Isomerases; C085868:PDIA3 protein, human