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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
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SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins

机译：SEL1L使错折叠的糖蛋白脱位所需的蛋白复合物成核

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摘要

Membrane and secretory proteins that fail to pass quality control in the endoplasmic reticulum are discharged into the cytosol and degraded by the proteasome. Many of the mammalian components involved in this process remain to be identified. We performed a biochemical search for proteins that interact with SEL1L, a protein that is part of the mammalian HRD1 ligase complex and involved in substrate recognition. SEL1L is crucial for dislocation of Class I major histocompatibility complex heavy chains by the human cytomegalovirus US11 protein. We identified AUP1, UBXD8, UBC6e, and OS9 as functionally important components of this degradation complex in mammalian cells, as confirmed by mu-tagenesis and dominant negative versions of these proteins.
机译：未能通过内质网质量控制的膜和分泌蛋白被排入细胞质并被蛋白酶体降解。此过程中涉及的许多哺乳动物成分仍有待确定。我们进行了与SEL1L相互作用的蛋白质的生化搜索，SEL1L是哺乳动物HRD1连接酶复合物的一部分，并参与底物识别。 SEL1L对于人巨细胞病毒US11蛋白使I类主要组织相容性复合物重链脱位至关重要。我们确定了AUP1，UBXD8，UBC6e和OS9是哺乳动物细胞中这种降解复合物的功能重要组成部分，这些蛋白的诱变作用和显性负性作用证实了这一点。

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