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SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins.

Authors
  • Mueller, Britta
  • Klemm, Elizabeth J
  • Spooner, Eric
  • Claessen, Jasper H
  • Ploegh, Hidde L
Type
Published Article
Journal
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Publication Date
Aug 26, 2008
Volume
105
Issue
34
Pages
12325–12330
Identifiers
DOI: 10.1073/pnas.0805371105
PMID: 18711132
Source
Medline
License
Unknown

Abstract

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.

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