Constitutive and interleukin-1-inducible phosphorylation of p65 NF-{kappa}B at serine 536 is mediated by multiple protein kinases including I{kappa}B kinase (IKK)-{alpha}, IKK{beta}, IKK{epsilon}, TRAF family member-associated (TANK)-binding kinase 1 (TBK1), and an unknown kinase and couples p65 to

@article{Buss2004ConstitutiveAI,
  title={Constitutive and interleukin-1-inducible phosphorylation of p65 NF-\{kappa\}B at serine 536 is mediated by multiple protein kinases including I\{kappa\}B kinase (IKK)-\{alpha\}, IKK\{beta\}, IKK\{epsilon\}, TRAF family member-associated (TANK)-binding kinase 1 (TBK1), and an unknown kinase and couples p65 to },
  author={Holger Buss and Anneke Doerrie and Michael Schmitz and Elke Hoffmann and Klaus Resch and Michael Kracht},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 53},
  pages={55633-43}
}
Phosphorylation of NF-kappaB p65(RelA) serine 536 is physiologically induced in response to a variety of proinflammatory stimuli, but the responsible pathways have not been conclusively unraveled, and the function of this phosphorylation is largely elusive. In contrast to previous studies, we found no evidence for a role of c-Jun N-terminal kinase, p38 kinase, extracellular signal-regulated kinase, or phosphatidylinositol 3-kinase in interleukin-1- or tumor necrosis factor-induced Ser-536… CONTINUE READING
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