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RPA interacts with XPA (xeroderma pigmentosum A) and functions in early stage of NER. We have shown that in cells the RPA\u2014XPA complex disassociated upon exposure of cells to high dose of UV irradiation. The dissociation required replication stress and was partially attributed to tRPA hyperphosphorylation. Treatment of cells with CPT (camptothecin) and HU (hydroxyurea), which cause DSB DNA damage and replication fork collapse respectively and also leads to the disruption of RPA\u2014XPA complex. Purified RPA and XPA were unable to form complex <jats:italic>in vitro<\/jats:italic> in the presence of ssDNA. We propose that the competition\u2010based RPA switch among different DNA metabolic pathways regulates the dissociation of RPA with XPA in cells after DNA damage. The biological significances of RPA\u2014XPA complex disruption in relation with checkpoint activation, DSB repair and RPA hyperphosphorylation are discussed.<\/jats:p>","DOI":"10.1042\/cbi20110633","type":"journal-article","created":{"date-parts":[[2012,5,14]],"date-time":"2012-05-14T08:22:53Z","timestamp":1336983773000},"page":"713-720","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Replication\u2010mediated disassociation of replication protein A\u2014XPA complex upon DNA damage: implications for RPA handing 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