15929725

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0012860, umls-concept:C0165675, umls-concept:C0475264, umls-concept:C1155874, umls-concept:C1158537, umls-concept:C1704241
pubmed:issue	Pt 3
pubmed:dateCreated	2005-10-21
pubmed:abstractText	RPA (replication protein A) is an essential factor for DNA DSB (double-strand break) repair and cell cycle checkpoint activation. The 32 kDa subunit of RPA undergoes hyperphosphorylation in response to cellular genotoxic insults. However, the potential involvement of hyperphosphorylated RPA in DSB repair and checkpoint activation remains unclear. Using co-immunoprecipitation assays, we showed that cellular interaction of RPA with two DSB repair factors, Rad51 and Rad52, was predominantly mediated by the hyperphosphorylated species of RPA in cells after UV and camptothecin treatment. Moreover, Rad51 and Rad52 displayed higher affinity for the hyperphosphorylated RPA than native RPA in an in vitro binding assay. Checkpoint kinase ATR (ataxia telangiectasia mutated and Rad3-related) also interacted more efficiently with the hyperphosphorylated RPA than with native RPA following DNA damage. Consistently, immunofluorescence microscopy demonstrated that the hyperphosphorylated RPA was able to co-localize with Rad52 and ATR to form significant nuclear foci in cells. Our results suggest that hyperphosphorylated RPA is preferentially localized to DSB repair and the DNA damage checkpoint complexes in response to DNA damage.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/CA86927, http://linkedlifedata.com/resource/pubmed/grant/R01 CA086927-04, http://linkedlifedata.com/resource/pubmed/grant/R01 CA086927-05
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2984726R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Rad51 Recombinase, http://linkedlifedata.com/resource/pubmed/chemical/Rad52 DNA Repair and Recombination..., http://linkedlifedata.com/resource/pubmed/chemical/Replication Protein A
pubmed:status	MEDLINE
pubmed:month	Nov
pubmed:issn	1470-8728
pubmed:author	pubmed-author:JinL ZLZ, pubmed-author:LiuYiyongY, pubmed-author:WuXiaomingX, pubmed-author:YangZhengguanZ
pubmed:issnType	Electronic
pubmed:day	1
pubmed:volume	391
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	473-80
pubmed:dateRevised	2011-5-24
pubmed:meshHeading	pubmed-meshheading:15929725-Adenocarcinoma, pubmed-meshheading:15929725-Cell Line, Tumor, pubmed-meshheading:15929725-DNA Damage, pubmed-meshheading:15929725-DNA Repair, pubmed-meshheading:15929725-Gene Expression Regulation, pubmed-meshheading:15929725-Humans, pubmed-meshheading:15929725-Lung Neoplasms, pubmed-meshheading:15929725-Phosphorylation, pubmed-meshheading:15929725-Protein Binding, pubmed-meshheading:15929725-Protein Transport, pubmed-meshheading:15929725-Rad51 Recombinase, pubmed-meshheading:15929725-Rad52 DNA Repair and Recombination Protein, pubmed-meshheading:15929725-Replication Protein A, pubmed-meshheading:15929725-Ultraviolet Rays
pubmed:year	2005
pubmed:articleTitle	Preferential localization of hyperphosphorylated replication protein A to double-strand break repair and checkpoint complexes upon DNA damage.
pubmed:affiliation	Department of Biochemistry and Molecular Biology, James H. Quillen College of Medicine, East Tennessee State University, Johnson City, TN 37614, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural