We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
HDAC4 deacetylase associates with and represses the MEF2 transcription factor.
- Authors
Miska, E A; Karlsson, C; Langley, E; Nielsen, S J; Pines, J; Kouzarides, T
- Abstract
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.
- Publication
The EMBO journal, 1999, Vol 18, Issue 18, p5099
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1093/emboj/18.18.5099