Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of IkappaBalpha.

@article{Tashiro1997DirectIO,
  title={Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of IkappaBalpha.},
  author={Kyoichi Tashiro and Matthew P. Pando and Yumi Kanegae and Penny Wamsley and Shinya Inou{\'e} and Inder M Verma},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1997},
  volume={94 15},
  pages={7862-7}
}
The NF-kappaB/Rel proteins are sequestered in the cytoplasm in association with IkappaBalpha. In response to external signals, IkappaBalpha is phosphorylated, multi-ubiquitinated, and degraded by proteasomes, thereby releasing NF-kappaB/Rel proteins to migrate to the nucleus. We have cloned a mouse ubiquitin-conjugating enzyme (mE2), which associates with IkappaBalpha. mE2 is homologous to the yeast Ubc9/Hus5 ubiquitin-conjugating enzyme. A transdominant-negative mutant of mE2 had no effect on… CONTINUE READING
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