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- Title
A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol.
- Authors
Ylhong Ye; Shlbata, Yoko; Chi Yun; Ron, David; Rapoport, Tom A.
- Abstract
Elimination 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 cofactor.
- Publication
Nature, 2004, Vol 429, Issue 6994, p841
- ISSN
0028-0836
- Publication type
Academic Journal
- DOI
10.1038/nature02656