Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha.

@article{Imbert1996TyrosinePO,
  title={Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha.},
  author={V{\'e}ronique Imbert and Rudolph A Rupec and Antonia Livolsi and Heike L Pahl and E B Traenckner and Christoph Mueller-Dieckmann and Dariush Farahifar and Bernard Rossi and Patrick Auberger and Patrick A. Baeuerle and J. F. Peyron},
  journal={Cell},
  year={1996},
  volume={86 5},
  pages={
          787-98
        }
}
The transcription factor NF-kappa B regulates genes participating in immune and inflammatory responses. In T lymphocytes, NF-kappa B is sequestered in the cytosol by the inhibitor I kappa B-alpha and released after serine phosphorylation of I kappa B-alpha that regulates its ubiquitin-dependent degradation. We report an alternative mechanism of NF-kappa B activation. Stimulation of Jurkat T cells with the protein tyrosine phosphatase inhibitor and T cell activator pervanadate led to NF-kappa B… CONTINUE READING
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