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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol.

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.

Pubmed ID: 15215856

Authors

  • Ye Y
  • Shibata Y
  • Yun C
  • Ron D
  • Rapoport TA

Journal

Nature

Publication Data

June 24, 2004

Associated Grants

None

Mesh Terms

  • Adenosine Triphosphatases
  • Amino Acid Sequence
  • Animals
  • Cytosol
  • Dogs
  • Endoplasmic Reticulum
  • Histocompatibility Antigens Class I
  • Humans
  • Macromolecular Substances
  • Membrane Proteins
  • Molecular Sequence Data
  • Nuclear Proteins
  • Protein Folding
  • Protein Processing, Post-Translational
  • Protein Transport
  • RNA-Binding Proteins
  • Selenoproteins
  • Viral Proteins