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http://purl.uniprot.org/citations/18614045http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18614045http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18614045http://www.w3.org/2000/01/rdf-schema#comment"The histone H2A variant H2AX is rapidly phosphorylated in response to DNA double-stranded breaks to produce gamma-H2AX. gamma-H2AX stabilizes cell-cycle checkpoint proteins and DNA repair factors at the break site. We previously found that the protein phosphatase PP2A is required to resolve gamma-H2AX foci and complete DNA repair after exogenous DNA damage. Here we describe a three-protein PP4 phosphatase complex in mammalian cells, containing PP4C, PP4R2, and PP4R3beta, that specifically dephosphorylates ATR-mediated gamma-H2AX generated during DNA replication. PP4 efficiently dephosphorylates gamma-H2AX within mononucleosomes in vitro and does not directly alter ATR or checkpoint kinase activity, suggesting that PP4 acts directly on gamma-H2AX in cells. When the PP4 complex is silenced, repair of DNA replication-mediated breaks is inefficient, and cells are hypersensitive to DNA replication inhibitors, but not radiomimetic drugs. Therefore, gamma-H2AX elimination at DNA damage foci is required for DNA damage repair, but accomplishing this task involves distinct phosphatases with potentially overlapping roles."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2008.05.016"xsd:string
http://purl.uniprot.org/citations/18614045http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2008.05.016"xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Chowdhury D."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Chowdhury D."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Xu X."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Xu X."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Zhong J."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Zhong J."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Liao J."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Liao J."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Zhong X."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Zhong X."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Pfeifer G.P."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Pfeifer G.P."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Lieberman J."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Lieberman J."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Ahmed F."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Ahmed F."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Weinstock D.M."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Weinstock D.M."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Dykxhoorn D.M."xsd:string
http://purl.uniprot.org/citations/18614045http://purl.uniprot.org/core/author"Dykxhoorn D.M."xsd:string