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| The EMBO Journal
(1999) 18, 5099–5107, doi:10.1093/emboj/18.18.5099 |
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| HDAC4 deacetylase associates with and represses the MEF2 transcription factor |
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| Eric A. Miska2, 1, Christina Karlsson3, 1, Emma Langley2, 1, Søren J. Nielsen2, 1, Jon Pines3, 1 and Tony Kouzarides2, 1 |
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1 Wellcome/CRC Institute, Tennis Court Road, Cambridge, UK 2 Department of Pathology, University of Cambridge, Cambridge, UK 3 Department of Zoology, University of Cambridge, Cambridge, UK To whom correspondence should be addressed Tony Kouzarides, tk106@mole.bio.cam.ac.uk Received 16 April 1999; Revised 11 June 1999; Accepted 27 July 1999. |
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| Abstract |
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| The acetylation state of histones can influence transcription. Acetylation, carried out by acetyltransferases such as CBP/p300 and P/CAF, is commonly associated with transcriptional stimulation, whereas deacetylation, mediated by the three known human deacetylases HDAC1, 2 and 3, causes transcriptional repression. The known human deacetylases represent a single family and are homologues of the yeast RPD3 deacetylase. Here we identify and characterize HDAC4, a representative of a new human histone deacetylase family, which is homologous to the yeast HDA1 deacetylase. We show that HDAC4, unlike other deacetylases, shuttles between the nucleus and the cytoplasm in a process involving active nuclear export. In the nucleus, HDAC4 associates with the myocyte enhancer factor MEF2A. Binding of HDAC4 to MEF2A results in the repression of MEF2A transcriptional activation, a function that requires the deacetylase domain of HDAC4. These results identify MEF2A as a nuclear target for HDAC4-mediated repression and suggests that compartmentalization may be a novel mechanism for controlling the nuclear activity of this new family of deacetylases. |
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| Keywords: HDAC4, HDA1, histone deacetylase, MEF2, nuclear export |
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