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Science 28 August 1998:
Vol. 281. no. 5381, pp. 1360 - 1363
DOI: 10.1126/science.281.5381.1360
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Reports

Direct Phosphorylation of Ikappa B by IKKalpha and IKKbeta : Discrimination Between Free and NF-kappa B-Bound Substrate

Ebrahim Zandi, * Yi Chen, * Michael Karin dagger

A large protein complex mediates the phosphorylation of the inhibitor of kappa B (Ikappa B), which results in the activation of nuclear factor kappa B (NF-kappa B). Two subunits of this complex, Ikappa B kinase alpha (IKKalpha ) and Ikappa B kinase beta  (IKKbeta ), are required for NF-kappa B activation. Purified recombinant IKKalpha and IKKbeta expressed in insect cells were used to demonstrate that each protein can directly phosphorylate Ikappa B proteins. IKKalpha and IKKbeta were found to form both homodimers and heterodimers. Both IKKalpha and IKKbeta phosphorylated Ikappa B bound to NF-kappa B more efficiently than they phosphorylated free Ikappa B. This result explains how free Ikappa B can accumulate in cells in which IKK is still active and thus can contribute to the termination of NF-kappa B activation.

Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
*   These authors contributed equally to this report.

dagger    To whom correspondence should be addressed. E-mail: karinoffice{at}ucsd.edu

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Aminosalicylic Acid Inhibits Ikappa B Kinase alpha Phosphorylation of Ikappa Balpha in Mouse Intestinal Epithelial Cells.
F. Yan and D. B. Polk (1999)
J. Biol. Chem. 274, 36631-36636
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The Human T-cell Leukemia Virus Type-1 Tax Protein Regulates the Activity of the Ikappa B Kinase Complex.
X. H. Li, K. M. Murphy, K. T. Palka, R. M. Surabhi, and R. B. Gaynor (1999)
J. Biol. Chem. 274, 34417-34424
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Primary Human CD4+ T Cells Contain Heterogeneous I{kappa}B Kinase Complexes: Role in Activation of the IL-2 Promoter.
A. Khoshnan, S. J. Kempiak, B. L. Bennett, D. Bae, W. Xu, A. M. Manning, C. H. June, and A. E. Nel (1999)
J. Immunol. 163, 5444-5452
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RelB Modulation of Ikappa Balpha Stability as a Mechanism of Transcription Suppression of Interleukin-1alpha (IL-1alpha ), IL-1beta , and Tumor Necrosis Factor Alpha in Fibroblasts.
Y. Xia, S. Chen, Y. Wang, N. Mackman, G. Ku, D. Lo, and L. Feng (1999)
Mol. Cell. Biol. 19, 7688-7696