Association of folding intermediates of glycoproteins with calnexin during protein maturation
- PMID: 8102790
- DOI: 10.1038/364771a0
Association of folding intermediates of glycoproteins with calnexin during protein maturation
Abstract
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.
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