Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome.

@article{Hughes1997MisfoldedMH,
  title={Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome.},
  author={Eric A. Hughes and Craig D. Hammond and Peter Cresswell},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1997},
  volume={94 5},
  pages={1896-901}
}
N-acetyl-L-leucyl-L-leucyl-L-norleucinal (LLnL), which reversibly inhibits the proteasome in addition to other proteases, and a more specific irreversible inhibitor of the proteasome, lactacystin, were found to cause the accumulation of major histocompatibility complex (MHC) class I heavy chains in the cytosol of the beta2-microglobulin-deficient cell line Daudi and the TAP-deficient cell line .174. These cell lines, which are severely impaired in their ability to fold MHC class I heavy chain… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 88 extracted citations

Similar Papers

Loading similar papers…