Journal
FEMS YEAST RESEARCH
Volume 4, Issue 8, Pages 815-820Publisher
OXFORD UNIV PRESS
DOI: 10.1016/j.femsyr.2004.04.002
Keywords
ERAD; protein quality control; Der7p; alpha-glucosidase I; Cwh41p
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Proteins entering the endoplasmic reticulum (ER) have to acquire an export-competent structure before they are delivered to their final destination. This folding process is monitored by an ER protein quality control system. Folding-incompetent conformers are eliminated via a mechanism called ER-associated protein degradation (ERAD). Genetic studies in the yeast Saccharomyces cerevisiae have revealed that carbohydrate modification plays a crucial role in these processes. Here we show that a previously isolated der mutant (der7-1) is defective in ERAD. We identify DER7 as the gene encoding N-glycan-processing alpha-glucosidase I (EC 3.2.1.106) of the ER and demonstrate that its inactivity, due to a substitution of the conserved glycine residue at position 725 by arginine (G725R) in the der7-1 mutant, leads to ER-stress. (C) 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
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