Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.

@article{Ye2005RecruitmentOT,
  title={Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.},
  author={Yihong Ye and Yoko Shibata and Marjolein Kikkert and Sjaak van Voorden and Emmanuel J H J Wiertz and Tom A Rapoport},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 40},
  pages={14132-8}
}
Misfolded proteins are eliminated from the endoplasmic reticulum (ER) by retrotranslocation into the cytosol, a pathway hijacked by certain viruses to destroy MHC class I heavy chains. The translocation of polypeptides across the ER membrane requires their polyubiquitination and subsequent extraction from the membrane by the p97 ATPase [also called valosin-containing protein (VCP) or, in yeast, Cdc48]. In higher eukaryotes, p97 is bound to the ER membrane by a membrane protein complex… CONTINUE READING
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