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A membrane protein required for dislocation of misfolded proteins from the ER

机译：错位蛋白从ER中脱位所需的膜蛋白

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After insertion into the endoplasmic reticulum ( ER), proteins that fail to fold there are destroyed. Through a process termed dislocation such misfolded proteins arrive in the cytosol, where ubiquitination, deglycosylation and finally proteasomal proteolysis dispense with the unwanted polypeptides. The machinery involved in the extraction of misfolded proteins from the ER is poorly defined. The human cytomegalovirus-encoded glycoproteins US2 and US11 catalyse the dislocation of class I major histocompatibility complex (MHC) products, resulting in their rapid degradation. Here we show that US11 uses its transmembrane domain to recruit class I MHC products to a human homologue of yeast Der1p, a protein essential for the degradation of a subset of misfolded ER proteins. We show that this protein, Derlin-1, is essential for the degradation of class I MHC molecules catalysed by US11, but not by US2. We conclude that Derlin-1 is an important factor for the extraction of certain aberrantly folded proteins from the mammalian ER.
机译：插入内质网（ER）后，无法在此处折叠的蛋白质将被破坏。通过称为位错的过程，这些错误折叠的蛋白质到达细胞质中，在那里泛素化，去糖基化和最后的蛋白酶体蛋白水解省去了不需要的多肽。从ER中提取错误折叠的蛋白质所涉及的机制定义不清。人类巨细胞病毒编码的糖蛋白US2和US11催化I类主要组织相容性复合物（MHC）产品的脱位，导致其快速降解。在这里，我们显示了US11使用其跨膜结构域将I类MHC产品募集到酵母Der1p的人类同源物中，Der1p是降解错误折叠的ER蛋白的子集所必需的蛋白。我们表明，这种蛋白Derlin-1，对于US11而非US2催化的I类MHC分子的降解至关重要。我们得出结论，Derlin-1是从哺乳动物ER中提取某些异常折叠蛋白的重要因素。

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