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      A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB.

      Nature
      Amino Acid Sequence, Cloning, Molecular, Enzyme Activation, HeLa Cells, Humans, I-kappa B Kinase, Inflammation Mediators, metabolism, Kinetics, Molecular Sequence Data, NF-kappa B, Phosphoprotein Phosphatases, Phosphorylation, Protein-Serine-Threonine Kinases, genetics, isolation & purification, Substrate Specificity, Tumor Necrosis Factor-alpha

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          Abstract

          Nuclear transcription factors of the NF-kappaB/Rel family are inhibited by IkappaB proteins, which inactivate NF-kappaB by trapping it in the cell cytoplasm. Phosphorylation of IkappaBs marks them out for destruction, thereby relieving their inhibitory effect on NF-kappaB. A cytokine-activated protein kinase complex, IKK (for IkappaB kinase), has now been purified that phosphorylates IkappaBs on the sites that trigger their degradation. A component of IKK was molecularly cloned and identified as a serine kinase. IKK turns out to be the long-sought-after protein kinase that mediates the critical regulatory step in NF-kappaB activation.

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