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Science 31 August 2001:
Vol. 293. no. 5535, pp. 1653 - 1657
DOI: 10.1126/science.1062374
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Reports

Duration of Nuclear NF-kappa B Action Regulated by Reversible Acetylation

Lin-feng Chen,1 Wolfgang Fischle,1 Eric Verdin,12 Warner C. Greene123*

The nuclear expression and action of the nuclear factor kappa B (NF-kappa B) transcription factor requires signal-coupled phosphorylation and degradation of the Ikappa B inhibitors, which normally bind and sequester this pleiotropically active factor in the cytoplasm. The subsequent molecular events that regulate the termination of nuclear NF-kappa B action remain poorly defined, although the activation of de novo Ikappa Balpha gene expression by NF-kappa B likely plays a key role. Our studies now demonstrate that the RelA subunit of NF-kappa B is subject to inducible acetylation and that acetylated forms of RelA interact weakly, if at all, with Ikappa Balpha . Acetylated RelA is subsequently deacetylated through a specific interaction with histone deacetylase 3 (HDAC3). This deacetylation reaction promotes effective binding to Ikappa Balpha and leads in turn to Ikappa Balpha -dependent nuclear export of the complex through a chromosomal region maintenance-1 (CRM-1)-dependent pathway. Deacetylation of RelA by HDAC3 thus acts as an intranuclear molecular switch that both controls the duration of the NF-kappa B transcriptional response and contributes to the replenishment of the depleted cytoplasmic pool of latent NF-kappa B-Ikappa Balpha complexes.

1 Gladstone Institute of Virology and Immunology,
2 Department of Medicine,
3 Department of Microbiology and Immunology, University of California, San Francisco, CA 94141, USA.
*   To whom correspondence should be addressed. E-mail: wgreene{at}gladstone.ucsf.edu

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Centrosomal P4.1-associated Protein Is a New Member of Transcriptional Coactivators for Nuclear Factor-{kappa}B.
M. Koyanagi, M. Hijikata, K. Watashi, O. Masui, and K. Shimotohno (2005)
J. Biol. Chem. 280, 12430-12437
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Chromatin Modification and the Endothelial-specific Activation of the E-selectin Gene.
L. C. Edelstein, A. Pan, and T. Collins (2005)
J. Biol. Chem. 280, 11192-11202
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Histone acetylation and deacetylation: importance in inflammatory lung diseases.
P. J. Barnes, I. M. Adcock, and K. Ito (2005)
Eur. Respir. J. 25, 552-563
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Tyrosine Nitration on p65: A Novel Mechanism to Rapidly Inactivate Nuclear Factor-{kappa}B.
S. W. Park, M. D.M. Huq, X. Hu, and L.-N. Wei (2005)
Mol. Cell. Proteomics 4, 300-309
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Histone Deacetylase Inhibition Down-Regulates Cyclin D1 Transcription by Inhibiting Nuclear Factor-{kappa}B/p65 DNA Binding.
J. Hu and N. H. Colburn (2005)
Mol. Cancer Res. 3, 100-109
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