Negative regulation of NF-κB p65 activity by serine 536 phosphorylation

@article{Pradre2016NegativeRO,
  title={Negative regulation of NF-κB p65 activity by serine 536 phosphorylation},
  author={Jean-Philippe Prad{\`e}re and C{\'e}line Hernandez and Christiane Koppe and Richard A. Friedman and Tom Luedde and Robert F. Schwabe},
  journal={Science Signaling},
  year={2016},
  volume={9},
  pages={ra85-ra85}
}
Nuclear factor κB (NF-κB) is a master regulator of inflammation and cell death. Whereas most of the activity of NF-κB is regulated through the inhibitor of κB (IκB) kinase (IKK)–dependent degradation of IκB, IKK also phosphorylates subunits of NF-κB. We investigated the contribution of the phosphorylation of the NF-κB subunit p65 at the IKK phosphorylation site serine 536 (Ser536) in humans, which is thought to be required for the activation and nuclear translocation of NF-κB. Through… CONTINUE READING
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Missing Pieces in the NF-κB Puzzle

View 5 Excerpts
Highly Influenced

Phosphorylation of serine 468 by GSK-3beta negatively regulates basal p65 NF-kappaB activity.

The Journal of biological chemistry • 2004
View 9 Excerpts
Highly Influenced

Role of Ca 2 + / calmodulin - dependent kinase II – IRAK 1 interaction in LMP 1 - induced NFk B activation

K.-Y. Jen, V. Soni, E. Kieff, E. Cahir-McFarland
Mol . Cell . Biol . • 2014

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