DER7, encoding alpha-glucosidase I is essential for degradation of malfolded glycoproteins of the endoplasmic reticulum.
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.[1]References
- DER7, encoding alpha-glucosidase I is essential for degradation of malfolded glycoproteins of the endoplasmic reticulum. Hitt, R., Wolf, D.H. FEMS Yeast Res. (2004) [Pubmed]
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