Open AccessDER7, encoding α‐glucosidase I is essential for degradation of malfolded glycoproteins of the endoplasmic reticulum
Author(s) -
Hitt Reiner,
Wolf Dieter H.
Publication year - 2004
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1016/j.femsyr.2004.04.002
Subject(s) - endoplasmic reticulum associated protein degradation , endoplasmic reticulum , biology , calnexin , glycan , saccharomyces cerevisiae , protein folding , mutant , glycoprotein , biochemistry , golgi apparatus , microbiology and biotechnology , unfolded protein response , yeast , gene , calreticulin
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 α‐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.