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Sci. STKE, 4 September 2001
Vol. 2001, Issue 98, p. tw5
[DOI: 10.1126/scisignal.982001tw5]

EDITORS' CHOICE

Nucleocytoplasmic Transport Acetylation and Nuclear Transport

The transcription factor NF-{kappa}B functions to control gene expression in immune and inflammatory responses and to control susceptibility of cells to apoptosis. It is therefore not surprising to find that multiple layers of regulation exist to control the activity of NF-{kappa}B and its movement into and out of the nucleus. NF-{kappa}B is normally held in an inactive state in the cytoplasm by interacting with the I{kappa}B protein. Signals that activate NF-{kappa}B cause degradation of I{kappa}B and translocation of active NF-{kappa}B to the nucleus. Now Chen et al. indicate that another layer of regulation is superimposed on this regulation by I{kappa}B. They show that interaction of NF-{kappa}B with I{kappa}B is disrupted when the NF-{kappa}B subunit RelA is acetylated. In the nucleus, deacetylation of the RelA protein by histone deacetylase 3 (HDAC3) leads to its reassociation with I{kappa}B and consequent transport out of the nucleus. Thus, HDAC3, which also regulates transcription through deacetylation of histones, influences both the activity and cellular localization of the NF-{kappa}B complex.

L. Chen, W. Fischle, E. Verdin, W. C. Greene, Duration of nuclear NF-{kappa}B action regulated by reversible acetylation. Science 293, 1653-1657. [Abstract] [Full Text]

Citation: Acetylation and Nuclear Transport. Sci. STKE 2001, tw5 (2001).

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