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http://purl.uniprot.org/citations/10487761http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10487761http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10487761http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.org/dc/terms/identifier"doi:10.1093/emboj/18.18.5099"xsd:string
http://purl.uniprot.org/citations/10487761http://purl.org/dc/terms/identifier"doi:10.1093/emboj/18.18.5099"xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Kouzarides T."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Kouzarides T."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Langley E."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Langley E."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Miska E.A."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Miska E.A."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Karlsson C."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Karlsson C."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Pines J."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Pines J."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Nielsen S.J."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/author"Nielsen S.J."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/pages"5099-5107"xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/pages"5099-5107"xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/title"HDAC4 deacetylase associates with and represses the MEF2 transcription factor."xsd:string
http://purl.uniprot.org/citations/10487761http://purl.uniprot.org/core/title"HDAC4 deacetylase associates with and represses the MEF2 transcription factor."xsd:string