Ubiquitination of lysine-331 by Kaposi's sarcoma-associated herpesvirus protein K5 targets HFE for lysosomal degradation.

@article{Rhodes2010UbiquitinationOL,
  title={Ubiquitination of lysine-331 by Kaposi's sarcoma-associated herpesvirus protein K5 targets HFE for lysosomal degradation.},
  author={David A. Rhodes and Louise H Boyle and Jessica M. Boname and Paul J Lehner and John Trowsdale},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 37},
  pages={16240-5}
}
The nonclassical MHC class I-related (MHC-I) molecule HFE controls cellular iron homeostasis by a mechanism that has not been fully elucidated. We examined the regulation of HFE by K5, the E3 ubiquitin ligase encoded by Kaposi's sarcoma-associated herpesvirus (KSHV/HHV8), that is known to down-regulate classical MHC-I. K5 down-regulated HFE efficiently, using polyubiquitination of the membrane proximal lysine in the HFE cytoplasmic tail (K331), to target the molecule for degradation via ESCRT1… CONTINUE READING