PubMed:15215856 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/15215856","sourcedb":"PubMed","sourceid":"15215856","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/15215856","text":"A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol.\nElimination of misfolded proteins from the endoplasmic reticulum (ER) by retro-translocation is an important physiological adaptation to ER stress. This process requires recognition of a substrate in the ER lumen and its subsequent movement through the membrane by the cytosolic p97 ATPase. Here we identify a p97-interacting membrane protein complex in the mammalian ER that links these two events. The central component of the complex, Derlin-1, is a homologue of Der1, a yeast protein whose inactivation prevents the elimination of misfolded luminal ER proteins. Derlin-1 associates with different substrates as they move through the membrane, and inactivation of Derlin-1 in C. elegans causes ER stress. Derlin-1 interacts with US11, a virally encoded ER protein that specifically targets MHC class I heavy chains for export from the ER, as well as with VIMP, a novel membrane protein that recruits the p97 ATPase and its 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