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| pubmed-article:15380617 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:15380617 | lifeskim:mentions | umls-concept:C1704708 | lld:lifeskim |
| pubmed-article:15380617 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:15380617 | lifeskim:mentions | umls-concept:C1424448 | lld:lifeskim |
| pubmed-article:15380617 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
| pubmed-article:15380617 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15380617 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:15380617 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:15380617 | pubmed:dateCreated | 2004-9-21 | lld:pubmed |
| pubmed-article:15380617 | pubmed:abstractText | Chk2 is a key player of the DNA damage signalling pathway. To identify new regulators of this kinase, we performed a yeast two-hybrid screen and found that Chk2 associated with the B' regulatory subunit of protein phosphatase PP2A. In vitro GST-Chk2 pulldowns demonstrated that B'gamma isoforms bound to Chk2 with the strongest apparent affinity. This was confirmed in cellulo by co-immunoprecipitation after overexpression of the respective partners in HEK293 cells. The A and C subunits of PP2A were present in the complexes, suggesting that Chk2 was associated with a functionnal PP2A. In vitro kinase assays showed that B'gamma3 was a potent Chk2 substrate. This phosphorylation increased the catalytic phosphatase activity of PP2A measured on MAP kinase-phosphorylated myelin basic protein as well as on autophosphorylated Chk2. Finally, we demonstrated that overexpressing B'gamma3 in HEK293 suppressed the phosphorylation of Chk2 induced by a genotoxic treatment, suggesting that PP2A may counteract the action of the checkpoint kinase in living cells. | lld:pubmed |
| pubmed-article:15380617 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15380617 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15380617 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15380617 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15380617 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15380617 | pubmed:issn | 0248-4900 | lld:pubmed |
| pubmed-article:15380617 | pubmed:author | pubmed-author:DarbonJean-Ma... | lld:pubmed |
| pubmed-article:15380617 | pubmed:author | pubmed-author:BaricaultLaur... | lld:pubmed |
| pubmed-article:15380617 | pubmed:author | pubmed-author:BonyadiMortaz... | lld:pubmed |
| pubmed-article:15380617 | pubmed:author | pubmed-author:DozierChristi... | lld:pubmed |
| pubmed-article:15380617 | pubmed:author | pubmed-author:TonassoLaureL | lld:pubmed |
| pubmed-article:15380617 | pubmed:copyrightInfo | Copyright 2004 Elsevier SAS | lld:pubmed |
| pubmed-article:15380617 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15380617 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:15380617 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15380617 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15380617 | pubmed:pagination | 509-17 | lld:pubmed |
| pubmed-article:15380617 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:15380617 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15380617 | pubmed:articleTitle | Regulation of Chk2 phosphorylation by interaction with protein phosphatase 2A via its B' regulatory subunit. | lld:pubmed |
| pubmed-article:15380617 | pubmed:affiliation | Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération, UMR 5088 CNRS, Institut Fédératif de Recherche 109, Université Paul Sabatier, Bât 4R3-B1, 118 route de Narbonne, 31062 Toulouse, France. dozier@cict.fr | lld:pubmed |
| pubmed-article:15380617 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15380617 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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