Association of folding intermediates of glycoproteins with calnexin during protein maturation.
Calnexin, an endoplasmic reticulum transmembrane protein, represents a new type of molecular chaperone that selectively associates in a transient fashion with newly synthesized monomeric glycoproteins in HepG2 cells. Calnexin only recognizes glycoproteins when they are incompletely folded. Dissociation of glycoproteins from calnexin occurs at different rates and is related to the time taken for their folding, which may then initiate their differential transport rates from the endoplasmic reticulum.
Ou
W J
WJ
Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.
Cameron
P H
PH
Thomas
D Y
DY
Bergeron
J J
JJ
D000418:Albumins / Q000378:metabolism; D001692:Biological Transport; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D037281:Calnexin; D002460:Cell Line; D018833:Chaperonins; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism*; D014168:Transferrin / Q000378:metabolism; D014415:Tunicamycin / Q000494:pharmacology; D000515:alpha 1-Antitrypsin / Q000378:metabolism
D000418:Albumins; D002135:Calcium-Binding Proteins; D006023:Glycoproteins; D011506:Proteins; D014168:Transferrin; D000515:alpha 1-Antitrypsin; D014415:Tunicamycin; D037281:Calnexin; D018833:Chaperonins