| http://purl.uniprot.org/citations/17928296 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17928296 | http://www.w3.org/2000/01/rdf-schema#comment | "The activity of human replication protein A (RPA) in DNA replication and repair is regulated by phosphorylation of the middle RPA2 subunit. It has previously been shown that up to nine different N-terminal residues are modified in vivo and in response to genotoxic stress. Using a novel antibody against phospho-Ser(29), a moiety formed by cyclin-Cdk, we observed that RPA2 was phosphorylated during mitosis in nonstressed cells. Robust phosphorylation of Ser(29) was also seen in interphase cells following treatment with the DNA-damaging agent camptothecin, a rare example of stress stimulating the modification of a repair factor by cyclin-Cdk. RPA2 phosphorylation is regulated both in cis and trans. Cis-phosphorylation follows a preferred pathway. (That is, the initial modification of Ser(33) by ATR stimulates subsequent phosphorylation of Cdk sites Ser(23) and Ser(29)). These events then facilitate modification of Thr(21) and extreme N-terminal sites Ser(4) and Ser(8), probably by DNA-PK. Our data also indicate that the phosphorylation of one RPA molecule can influence the phosphorylation of other RPA molecules in trans. Cells in which endogenous RPA2 was "replaced" with a double S23A/S29A-RPA2 mutant were seen to have an abnormal cell cycle distribution both in normal and in stressed cells. Such cells also showed aberrant DNA damage-dependent RPA foci and had persistent staining of gammaH2AX following DNA damage. Our data indicate that RPA phosphorylation facilitates chromosomal DNA repair. We postulate that the RPA phosphorylation pattern provides a means to regulate the DNA repair pathway utilized."xsd:string |
| http://purl.uniprot.org/citations/17928296 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m704645200"xsd:string |
| http://purl.uniprot.org/citations/17928296 | http://purl.uniprot.org/core/author | "Vassin V.M."xsd:string |
| http://purl.uniprot.org/citations/17928296 | http://purl.uniprot.org/core/author | "Borowiec J.A."xsd:string |
| http://purl.uniprot.org/citations/17928296 | http://purl.uniprot.org/core/author | "Anantha R.W."xsd:string |
| http://purl.uniprot.org/citations/17928296 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17928296 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/17928296 | http://purl.uniprot.org/core/pages | "35910-35923"xsd:string |
| http://purl.uniprot.org/citations/17928296 | http://purl.uniprot.org/core/title | "Sequential and synergistic modification of human RPA stimulates chromosomal DNA repair."xsd:string |
| http://purl.uniprot.org/citations/17928296 | http://purl.uniprot.org/core/volume | "282"xsd:string |
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