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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.<\/jats:p>","DOI":"10.1073\/pnas.0708455105","type":"journal-article","created":{"date-parts":[[2008,3,13]],"date-time":"2008-03-13T21:27:12Z","timestamp":1205443632000},"page":"4727-4732","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":71,"title":["Protein phosphatase 2A controls the activity of histone deacetylase 7 during T cell apoptosis and angiogenesis"],"prefix":"10.1073","volume":"105","author":[{"given":"Maud","family":"Martin","sequence":"first","affiliation":[{"name":"*Cellular and Molecular Biology Unit, FUSAGx, 5030 Gembloux, Belgium;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Potente","sequence":"additional","affiliation":[{"name":"Molecular Cardiology, Department of Internal Medicine III, University of Frankfurt, 60590 Frankfurt, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Veerle","family":"Janssens","sequence":"additional","affiliation":[{"name":"Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit Leuven, Campus Gasthuisberg O\/N1, 3000 Leuven, Belgium; 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