| First Author | Ye Y | Year | 2004 |
| Journal | Nature | Volume | 429 |
| Issue | 6994 | Pages | 841-7 |
| PubMed ID | 15215856 | Mgi Jnum | J:159067 |
| Mgi Id | MGI:4441126 | Doi | 10.1038/nature02656 |
| Citation | Ye Y, et al. (2004) A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429(6994):841-7 |
| abstractText | 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. |
