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

Author

Listed:
  • Yihong Ye

    (Harvard Medical School)

  • Yoko Shibata

    (Harvard Medical School)

  • Chi Yun

    (New York University School of Medicine)

  • David Ron

    (New York University School of Medicine)

  • Tom A. Rapoport

    (Harvard Medical School)

Abstract

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.

Suggested Citation

  • Yihong Ye & Yoko Shibata & Chi Yun & David Ron & Tom A. Rapoport, 2004. "A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol," Nature, Nature, vol. 429(6994), pages 841-847, June.
    • Handle: RePEc:nat:nature:v:429:y:2004:i:6994:d:10.1038_nature02656
    DOI: 10.1038/nature02656
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    Cited by:

    1. Yan Wang & Xiao Yang & Yong Zheng & Zhi-Hao Wu & Xiao-Ai Zhang & Qiu-Ping Li & Xi-Yu He & Chun-Zhi Wang & Zhi-Chun Feng, 2013. "The SEPS1 G-105A Polymorphism Is Associated with Risk of Spontaneous Preterm Birth in a Chinese Population," PLOS ONE, Public Library of Science, vol. 8(6), pages 1-7, June.

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