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• W2150590100 startingPage "1123" @default.
• W2150590100 abstract "Newly synthesized glycoproteins interact during folding and quality control in the ER with calnexin and calreticulin, two lectins specific for monoglucosylated oligosaccharides. Binding and release are regulated by two enzymes, glucosidase II and UDP-Glc:glycoprotein:glycosyltransferase (GT), which cyclically remove and reattach the essential glucose residues on the N-linked oligosaccharides. GT acts as a folding sensor in the cycle, selectively reglucosylating incompletely folded glycoproteins and promoting binding of its substrates to the lectins. To investigate how nonnative protein conformations are recognized and directed to this unique chaperone system, we analyzed the interaction of GT with a series of model substrates with well defined conformations derived from RNaseB. We found that conformations with slight perturbations were not reglucosylated by GT. In contrast, a partially structured nonnative form was efficiently recognized by the enzyme. When this form was converted back to a nativelike state, concomitant loss of recognition by GT occurred, reproducing the reglucosylation conditions observed in vivo with isolated components. Moreover, fully unfolded conformers were poorly recognized. The results indicated that GT is able to distinguish between different nonnative conformations with a distinct preference for partially structured conformers. The findings suggest that discrete populations of nonnative conformations are selectively reglucosylated to participate in the calnexin/calreticulin chaperone pathway." @default.
• W2150590100 created "2016-06-24" @default.
• W2150590100 creator A5031638977 @default.
• W2150590100 creator A5057675183 @default.
• W2150590100 date "2000-03-20" @default.
• W2150590100 modified "2023-10-18" @default.
• W2150590100 title "Conformational Requirements for Glycoprotein Reglucosylation in the Endoplasmic Reticulum" @default.
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• W2150590100 doi "https://doi.org/10.1083/jcb.148.6.1123" @default.
• W2150590100 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2174309" @default.
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• W2150590100 hasPublicationYear "2000" @default.
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