The ubiquitin ligase HERC3 attenuates NF-κB-dependent transcription independently of its enzymatic activity by delivering the RelA subunit for degradation

@inproceedings{Hochrainer2015TheUL,
  title={The ubiquitin ligase HERC3 attenuates NF-κB-dependent transcription independently of its enzymatic activity by delivering the RelA subunit for degradation},
  author={Karin Hochrainer and Nadja Pejanovic and Victoria A. Olaseun and Sheng Zhang and C Iadecola and Josef Anrather},
  booktitle={Nucleic acids research},
  year={2015}
}
Activation of NF-κB-dependent transcription represents an important hallmark of inflammation. While the acute inflammatory response is per se beneficial, it can become deleterious if its spatial and temporal profile is not tightly controlled. Classically, NF-κB activity is limited by cytoplasmic retention of the NF-κB dimer through binding to inhibitory IκB proteins. However, increasing evidence suggests that NF-κB activity can also be efficiently contained by direct ubiquitination of NF-κB… CONTINUE READING

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Inhibitor of growth 4 induces NFkappaB / p 65 ubiquitin - dependent degradation

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