Sci. STKE, 4 September 2001
Nucleocytoplasmic Transport Acetylation and Nuclear Transport
The transcription factor NF-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-B and its movement into and out of the nucleus. NF-B is normally held in an inactive state in the cytoplasm by interacting with the IB protein. Signals that activate NF-B cause degradation of IB and translocation of active NF-B to the nucleus. Now Chen et al. indicate that another layer of regulation is superimposed on this regulation by IB. They show that interaction of NF-B with IB is disrupted when the NF-B subunit RelA is acetylated. In the nucleus, deacetylation of the RelA protein by histone deacetylase 3 (HDAC3) leads to its reassociation with IB 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-B complex.
Citation: Acetylation and Nuclear Transport. Sci. STKE 2001, tw5 (2001).
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