Abstract
Rel/NF-κB transcription factors are primarily regulated by association with inhibitor IκB proteins. Thus, in most cells NF-κB exists in the cytoplasm in an inactive complex bound to IκB. Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB. The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex, whose catalysis is generally carried out by a heterodimeric kinase consisting of IKKα and IKKβ subunits. This review describes the identification of proteins in the IKK complex, and the regulation and physiological functions of IKK.
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Acknowledgements
I thank B Thompson for excellent manuscript assistance and M Delhase, Y Hu and D Rothwarf for discussions and artwork. Work in the author's laboratory is supported by the National Institutes of Health (NIEHS and NIAID) and the Department of Energy. M Karin is the Frank and Else Schilling-American Cancer Society Research Professor.
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Karin, M. How NF-κB is activated: the role of the IκB kinase (IKK) complex. Oncogene 18, 6867–6874 (1999). https://doi.org/10.1038/sj.onc.1203219
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DOI: https://doi.org/10.1038/sj.onc.1203219