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首页> 外文期刊>Nature >A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

机译：膜蛋白复合物介导从ER内腔逆向转运至细胞质

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摘要

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.
机译：通过逆向转运从内质网（ER）消除错误折叠的蛋白质是对ER应激的重要生理适应。此过程需要识别内质网腔中的底物，并随后通过胞质p97 ATPase通过膜移动。在这里，我们确定了哺乳动物ER中与这两个事件相关的p97相互作用膜蛋白复合物。该复合物的核心成分Derlin-1是Der1的同源物，Der1是一种酵母蛋白，其失活可以防止错误折叠的腔内ER蛋白的消除。当Derlin-1穿过膜时，它们会与不同的底物缔合，而线虫中Derlin-1的失活会引起ER应力。 Derlin-1与US11（一种病毒编码的ER蛋白）相互作用，该蛋白专门靶向从ER出口的MHC I类重链，还与VIMP（一种募集p97 ATPase及其辅因子的新型膜蛋白）相互作用。

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