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

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.

Pubmed ID: 9252186

Authors

  • DiDonato JA
  • Hayakawa M
  • Rothwarf DM
  • Zandi E
  • Karin M

Journal

Nature

Publication Data

August 7, 1997

Associated Grants

None

Mesh Terms

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