| pubmed-article:17210576 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C0031678 | lld:lifeskim |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C0085862 | lld:lifeskim |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C1299583 | lld:lifeskim |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C1332120 | lld:lifeskim |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C1332753 | lld:lifeskim |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C1608386 | lld:lifeskim |
| pubmed-article:17210576 | lifeskim:mentions | umls-concept:C1549571 | lld:lifeskim |
| pubmed-article:17210576 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:17210576 | pubmed:dateCreated | 2007-3-5 | lld:pubmed |
| pubmed-article:17210576 | pubmed:abstractText | ATM and Rad3-related (ATR) is a regulatory kinase that, when activated by hydroxyurea, UV, or human immunodeficiency virus-1 Vpr, causes cell cycle arrest through Chk1-Ser(345) phosphorylation. We demonstrate here that of these three agents only Vpr requires protein phosphatase type 2A (PP2A) to activate ATR for Chk1-Ser(345) phosphorylation. A requirement for PP2A by Vpr was first shown with the PP2A-specific inhibitor okadaic acid, which reduced Vpr-induced G(2) arrest and Cdk1-Tyr(15) phosphorylation. Using small interference RNA to down-regulate specific subunits of PP2A indicated that the catalytic beta-isoform PP2A(Cbeta) and the A regulatory alpha-isoform PP2A(Aalpha) are involved in the G(2) induction, and these downregulations decreased the Vpr-induced, ATR-dependent phosphorylations of Cdk1-Tyr(15) and Chk1-Ser(345). In contrast, the same down-regulations had no effect on hydroxyurea- or UV-activated ATR-dependent Chk1-Ser(345) phosphorylation. Vpr and hydroxyurea/UV all induce ATR-mediated gammaH2AX-Ser(139) phosphorylation and foci formation, but down-regulation of PP2A(Aalpha) or PP2A(Cbeta) did not decrease gammaH2AX-Ser(139) phosphorylation by any of these agents or foci formation by Vpr. Conversely, H2AX down-regulation had little effect on PP2A(Aalpha/Cbeta)-mediated G(2) arrest and Chk1-Ser(345) phosphorylation by Vpr. The expression of vpr increases the amount and phosphorylation of Claspin, an activator of Chk1 phosphorylation. Down-regulation of either PP2A(Cbeta) or PP2A(Aalpha) had little effect on Claspin phosphorylation, but the amount of Claspin was reduced. Claspin may then be one of the phosphoproteins through which PP2A(Aalpha/Cbeta) affects Chk1 phosphorylation when ATR is activated by human immunodeficiency virus-1 Vpr. | lld:pubmed |
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| pubmed-article:17210576 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17210576 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17210576 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17210576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17210576 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17210576 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:17210576 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17210576 | pubmed:author | pubmed-author:TYEV MVM | lld:pubmed |
| pubmed-article:17210576 | pubmed:author | pubmed-author:QinKefengK | lld:pubmed |
| pubmed-article:17210576 | pubmed:author | pubmed-author:ElderRobert... | lld:pubmed |
| pubmed-article:17210576 | pubmed:author | pubmed-author:DongLiangL | lld:pubmed |
| pubmed-article:17210576 | pubmed:author | pubmed-author:ParkHyeon... | lld:pubmed |
| pubmed-article:17210576 | pubmed:author | pubmed-author:ZhaoRichard... | lld:pubmed |
| pubmed-article:17210576 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17210576 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:17210576 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17210576 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17210576 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17210576 | pubmed:pagination | 7287-98 | lld:pubmed |
| pubmed-article:17210576 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:17210576 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17210576 | pubmed:articleTitle | Phosphatase type 2A-dependent and -independent pathways for ATR phosphorylation of Chk1. | lld:pubmed |
| pubmed-article:17210576 | pubmed:affiliation | Department of Pathology, Department of Microbiology-Immunology, Institute of Human Virology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA. | lld:pubmed |
| pubmed-article:17210576 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17210576 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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