AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation.

@article{Rabinovich2002AAAATPasePA,
  title={AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation.},
  author={Efrat Rabinovich and Anat Kerem and K U Fr{\"o}hlich and Noam Diamant and Shoshana Bar-Nun},
  journal={Molecular and cellular biology},
  year={2002},
  volume={22 2},
  pages={626-34}
}
Endoplasmic reticulum-associated degradation (ERAD) disposes of aberrant proteins in the secretory pathway. Protein substrates of ERAD are dislocated via the Sec61p translocon from the endoplasmic reticulum to the cytosol, where they are ubiquitinated and degraded by the proteasome. Since the Sec61p channel is also responsible for import of nascent proteins, this bidirectional passage should be coordinated, probably by molecular chaperones. Here we implicate the cytosolic chaperone AAA-ATPase… CONTINUE READING
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