| pubmed-article:18339811 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18339811 | lifeskim:mentions | umls-concept:C0302600 | lld:lifeskim |
| pubmed-article:18339811 | lifeskim:mentions | umls-concept:C1704708 | lld:lifeskim |
| pubmed-article:18339811 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:18339811 | lifeskim:mentions | umls-concept:C1422387 | lld:lifeskim |
| pubmed-article:18339811 | lifeskim:mentions | umls-concept:C2610891 | lld:lifeskim |
| pubmed-article:18339811 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:18339811 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:18339811 | pubmed:dateCreated | 2008-3-26 | lld:pubmed |
| pubmed-article:18339811 | pubmed:abstractText | Class IIa histone deacetylases (HDACs) act as key transcriptional regulators in several important developmental programs. Their activities are controlled via phosphorylation-dependent nucleocytoplasmic shuttling. Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. Although a lot of effort has been made toward the identification of the inactivating kinases that phosphorylate class IIa HDAC 14-3-3 motifs, the existence of an antagonistic protein phosphatase remains elusive. Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs. Interestingly, dephosphorylation of class IIa HDACs by PP2A is prevented by competitive association of 14-3-3 proteins. Using both okadaic acid treatment and RNA interference, we demonstrate that PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions. This study unravels a dynamic interplay among 14-3-3s, protein kinases, and PP2A and provides a model for the regulation of class IIa HDACs. | lld:pubmed |
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| pubmed-article:18339811 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18339811 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18339811 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18339811 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18339811 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:18339811 | pubmed:author | pubmed-author:KettmannRicha... | lld:pubmed |
| pubmed-article:18339811 | pubmed:author | pubmed-author:DimmelerStefa... | lld:pubmed |
| pubmed-article:18339811 | pubmed:author | pubmed-author:DequiedtFranc... | lld:pubmed |
| pubmed-article:18339811 | pubmed:author | pubmed-author:PotenteMichae... | lld:pubmed |
| pubmed-article:18339811 | pubmed:author | pubmed-author:GorisJozefJ | lld:pubmed |
| pubmed-article:18339811 | pubmed:author | pubmed-author:VertommenDidi... | lld:pubmed |
| pubmed-article:18339811 | pubmed:author | pubmed-author:RiderMark HMH | lld:pubmed |
| pubmed-article:18339811 | pubmed:author | pubmed-author:JanssensVeerl... | lld:pubmed |
| pubmed-article:18339811 | pubmed:author | pubmed-author:TwizereJean-C... | lld:pubmed |
| pubmed-article:18339811 | pubmed:author | pubmed-author:MartinMaudM | lld:pubmed |
| pubmed-article:18339811 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18339811 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:18339811 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:18339811 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18339811 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18339811 | pubmed:pagination | 4727-32 | lld:pubmed |
| pubmed-article:18339811 | pubmed:dateRevised | 2009-12-11 | lld:pubmed |
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| pubmed-article:18339811 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18339811 | pubmed:articleTitle | Protein phosphatase 2A controls the activity of histone deacetylase 7 during T cell apoptosis and angiogenesis. | lld:pubmed |
| pubmed-article:18339811 | pubmed:affiliation | Cellular and Molecular Biology Unit, FUSAGx, 5030 Gembloux, Belgium. | lld:pubmed |
| pubmed-article:18339811 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18339811 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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