Editors' ChoiceNucleocytoplasmic Transport

Acetylation and Nuclear Transport

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Science's STKE  04 Sep 2001:
Vol. 2001, Issue 98, pp. tw5
DOI: 10.1126/stke.2001.98.tw5

The transcription factor NF-κB 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-κB and its movement into and out of the nucleus. NF-κB is normally held in an inactive state in the cytoplasm by interacting with the IκB protein. Signals that activate NF-κB cause degradation of IκB and translocation of active NF-κB to the nucleus. Now Chen et al. indicate that another layer of regulation is superimposed on this regulation by IκB. They show that interaction of NF-κB with IκB is disrupted when the NF-κB subunit RelA is acetylated. In the nucleus, deacetylation of the RelA protein by histone deacetylase 3 (HDAC3) leads to its reassociation with IκB 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-κB complex.

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

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