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A cytokine-responsive IκB kinase that activates the transcription factor NF-κB

Author

Listed:
  • Joseph A. DiDonato
  • Makio Hayakawa
  • David M. Rothwarf
  • Ebrahim Zandi
  • Michael Karin

    (Laboratory of Gene Regulation and Signal Transduction, University of California at San Diego)

Abstract

Nuclear transcription factors of the NF-κB/Rel family are inhibited by IκB proteins, which inactivate NF-κB by trapping it in the cell cytoplasm. Phosphorylation of IκBs marks them out for destruction, thereby relieving their inhibitory effect on NF-κB. A cytokine-activated protein kinase complex, IKK (for IκB kinase), has now been purified that phosphorylates IκBs 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-κB activation.

Suggested Citation

  • Joseph A. DiDonato & Makio Hayakawa & David M. Rothwarf & Ebrahim Zandi & Michael Karin, 1997. "A cytokine-responsive IκB kinase that activates the transcription factor NF-κB," Nature, Nature, vol. 388(6642), pages 548-554, August.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6642:d:10.1038_41493
    DOI: 10.1038/41493
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