MHC class I molecules are preferentially ubiquitinated on endoplasmic reticulum luminal residues during HRD1 ubiquitin E3 ligase-mediated dislocation.

@article{Burr2013MHCCI,
  title={MHC class I molecules are preferentially ubiquitinated on endoplasmic reticulum luminal residues during HRD1 ubiquitin E3 ligase-mediated dislocation.},
  author={Marian L. Burr and Dick J. H. van den Boomen and Helen Bye and Robin Antrobus and Emmanuel J H J Wiertz and Paul J Lehner},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 35},
  pages={14290-5}
}
Misfolded MHC class I heavy chains (MHC I HCs) are targeted for endoplasmic reticulum (ER)-associated degradation (ERAD) by the ubiquitin E3 ligase HRD1, and E2 ubiquitin conjugating enzyme UBE2J1, and represent one of the few known endogenous ERAD substrates. The mechanism by which misfolded proteins are dislocated across the ER membrane into the cytosol is unclear. Here, we investigate the requirements for MHC I ubiquitination and degradation and show that endogenous misfolded MHC I HCs are… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 22 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 28 references

Similar Papers

Loading similar papers…