SEL 1L nucleates a protein complex required for dislocation of misfolded glycoproteins

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 intera...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2008-08, Vol.105 (34), p.12325
Hauptverfasser:	Mueller, Britta, Klemm, Elizabeth J, Spooner, Eric, Claessen, Jasper H, Ploegh, Hidde L
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Sprache:	eng
Schlagworte:	Glycoproteins Mammals Membranes Mutation Protein folding Proteomics
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creator	Mueller, Britta Klemm, Elizabeth J Spooner, Eric Claessen, Jasper H Ploegh, Hidde L
description	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 mutagenesis and dominant negative versions of these proteins.1 [PUBLICATION ABSTRACT]
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source	Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry
subjects	Glycoproteins Mammals Membranes Mutation Protein folding Proteomics
title	SEL 1L nucleates a protein complex required for dislocation of misfolded glycoproteins
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