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• W2141970640 abstract "The N-glycan-dependent quality control of glycoprotein folding prevents endoplasmic reticulum to Golgi exit of folding intermediates, irreparably misfolded glycoproteins and not completely assembled multimeric complexes. It also enhances folding efficiency by preventing aggregation and facilitating formation of proper disulfide bonds. The control mechanism essentially involves four components, resident lectin-chaperones that recognize monoglucosylated polymannose glycans, a lectin-associated oxidoreductase acting on monoglucosylated glycoproteins, a glucosyltransferase and a glucosidase that creates monoglucosylated epitopes in glycans transferred in protein N-glycosylation or removes the glucose units added by the glucosyltransferase. This last enzyme is the only mechanism component sensing glycoprotein conformations as it creates monoglucosylated glycans exclusively in not properly folded species or in not completely assembled complexes. The purpose of the review is to describe the most significant recent findings on the mechanism of glycoprotein folding and assembly quality control and to discuss the main still unanswered questions." @default.
• W2141970640 created "2016-06-24" @default.
• W2141970640 creator A5000229891 @default.
• W2141970640 creator A5071112170 @default.
• W2141970640 date "2007-12-01" @default.
• W2141970640 modified "2023-09-27" @default.
• W2141970640 title "How sugars convey information on protein conformation in the endoplasmic reticulum" @default.
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• W2141970640 doi "https://doi.org/10.1016/j.semcdb.2007.09.006" @default.
• W2141970640 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2196135" @default.
• W2141970640 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17997334" @default.
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