The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum.

@article{Claessen2010TheTS,
  title={The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum.},
  author={Jasper H. L. Claessen and Britta Katrin M{\"u}ller and Eric Spooner and Valerie L Pivorunas and Hidde L. Ploegh},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 27},
  pages={20732-9}
}
Terminally misfolded proteins that accumulate in the endoplasmic reticulum (ER) are dislocated and targeted for ubiquitin-dependent destruction by the proteasome. UBC6e is a tail-anchored E2 ubiquitin-conjugating enzyme that is part of a dislocation complex nucleated by the ER-resident protein SEL1L. Little is known about the turnover of tail-anchored ER proteins. We constructed a set of UBC6e transmembrane domain replacement mutants and found that the tail anchor of UBC6e is vital for its… CONTINUE READING

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