Dissecting the ER-Associated Degradation of a Misfolded Polytopic Membrane Protein

@article{Nakatsukasa2008DissectingTE,
  title={Dissecting the ER-Associated Degradation of a Misfolded Polytopic Membrane Protein},
  author={Kunio Nakatsukasa and Gregory Huyer and Susan Michaelis and Jeffrey L Brodsky},
  journal={Cell},
  year={2008},
  volume={132},
  pages={101-112}
}
It remains unclear how misfolded membrane proteins are selected and destroyed during endoplasmic reticulum-associated degradation (ERAD). For example, chaperones are thought to solubilize aggregation-prone motifs, and some data suggest that these proteins are degraded at the ER. To better define how membrane proteins are destroyed, the ERAD of Ste6p(*), a 12 transmembrane protein, was reconstituted. We found that specific Hsp70/40s act before ubiquitination and facilitate Ste6p(*) association… CONTINUE READING
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