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• W2104734239 abstract "Glycoprotein folding and degradation in the endoplasmic reticulum (ER) is mediated by the ER quality control system. Mannose trimming plays an important role by forming specific N-glycans that permit the recognition and sorting of terminally misfolded conformers for ERAD (ER-associated degradation). The EDEM (ER degradation enhancing α-mannosidase-like protein) subgroup of proteins belonging to the Class I α1,2-mannosidase family (glycosylhydrolase family 47) has been shown to enhance ERAD. We recently reported that overexpression of EDEM3 enhances glycoprotein ERAD with a concomitant increase in mannose-trimming activity in vivo. Herein, we report that overexpression of EDEM1 produces Glc1Man8GlcNAc2 isomer C on terminally misfolded null Hong Kong α1-antitrypsin (NHK) in vivo. Levels of this isomer increased throughout the chase period and comprised approximately 10% of the [3H]mannose-labeled N-glycans on NHK after a 3-h chase. Furthermore, overexpression of EDEM1 E220Q containing a mutation in a conserved catalytic residue essential for α1,2-mannosidase activity did not yield detectable levels of Glc1Man8GlcNAc2 isomer C. Yet, the same extent of NHK ERAD-enhancement was observed in both EDEM1 and EDEM1 E220Q overexpressing cells. This can be attributed to both wild-type and mutant EDEM1 inhibiting aberrant NHK dimer formation. We further analyzed the N-glycan profile of total cellular glycoproteins from HepG2 cells stably overexpressing EDEM1 and found that the relative amount of Man7GlcNAc2 isomer A, which lacks the terminal B and C branch mannoses, was increased compared to parental HepG2 cells. Based on this observation, we conclude that EDEM1 activity trims mannose from the C branch of N-glycans in vivo." @default.
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• W2104734239 date "2010-01-11" @default.
• W2104734239 modified "2023-10-11" @default.
• W2104734239 title "EDEM1 accelerates the trimming of 1,2-linked mannose on the C branch of N-glycans" @default.
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• W2104734239 doi "https://doi.org/10.1093/glycob/cwq001" @default.
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