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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
33
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pubmed:dateCreated |
2004-8-9
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pubmed:abstractText |
Class II histone deacetylases (HDACs) play a role in myogenesis and inhibit transcriptional activation by myocyte enhancer factors 2. A distinct feature of class II HDACs is their ability to shuttle between the nucleus and the cytoplasm in a cell type- and signal-dependent manner. We demonstrate here that treatment with the 26 S proteosome inhibitors, MG132 and ALLN, leads to detection of ubiquitinated HDAC7 and causes accumulation of cytoplasmic HDAC7. We also show that treatment with calyculin A, a protein phosphatase inhibitor, leads to a marked increase of HDAC7 but not HDAC5. The increase in HDAC7 is accompanied by enhanced interaction between 14-3-3 proteins and HDAC7. HDAC7 mutations that prevent the interaction with 14-3-3 proteins also block calyculin A-mediated stabilization. Expression of constitutively active calcium/calmodulin-dependent kinase I stabilizes HDAC7 and causes an increased association between HDAC7 and 14-3-3. Together, our results suggest that calcium/calmodulin-dependent kinase I-mediated phosphorylation of HDAC7 acts, in part, to promote association of HDAC7 with 14-3-3 and stabilizes HDAC7.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ATP dependent 26S protease,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/HDAC7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Histone Deacetylases,
http://linkedlifedata.com/resource/pubmed/chemical/Leupeptins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/acetylleucyl-leucyl-norleucinal,
http://linkedlifedata.com/resource/pubmed/chemical/benzyloxycarbonylleucyl-leucyl-leuci...,
http://linkedlifedata.com/resource/pubmed/chemical/calyculin A
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
34201-8
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pubmed:dateRevised |
2009-12-11
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pubmed:meshHeading |
pubmed-meshheading:15166223-14-3-3 Proteins,
pubmed-meshheading:15166223-Cell Line,
pubmed-meshheading:15166223-Cell Nucleus,
pubmed-meshheading:15166223-Cysteine Proteinase Inhibitors,
pubmed-meshheading:15166223-Cytoplasm,
pubmed-meshheading:15166223-Enzyme Inhibitors,
pubmed-meshheading:15166223-Histone Deacetylases,
pubmed-meshheading:15166223-Humans,
pubmed-meshheading:15166223-Leupeptins,
pubmed-meshheading:15166223-Models, Biological,
pubmed-meshheading:15166223-Mutation,
pubmed-meshheading:15166223-Oxazoles,
pubmed-meshheading:15166223-Peptide Hydrolases,
pubmed-meshheading:15166223-Phosphorylation,
pubmed-meshheading:15166223-Plasmids,
pubmed-meshheading:15166223-Proteasome Endopeptidase Complex,
pubmed-meshheading:15166223-Protein Binding,
pubmed-meshheading:15166223-Protein Biosynthesis,
pubmed-meshheading:15166223-Time Factors,
pubmed-meshheading:15166223-Transcription, Genetic,
pubmed-meshheading:15166223-Transcriptional Activation,
pubmed-meshheading:15166223-Transfection,
pubmed-meshheading:15166223-Tyrosine 3-Monooxygenase,
pubmed-meshheading:15166223-Up-Regulation
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pubmed:year |
2004
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pubmed:articleTitle |
Phosphorylation of the histone deacetylase 7 modulates its stability and association with 14-3-3 proteins.
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pubmed:affiliation |
Department of Biochemistry, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Cleveland, OH 44106, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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