{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,10]],"date-time":"2025-09-10T22:55:48Z","timestamp":1757544948620},"reference-count":59,"publisher":"Wiley","issue":"19","license":[{"start":{"date-parts":[[2013,8,27]],"date-time":"2013-08-27T00:00:00Z","timestamp":1377561600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2013,10]]},"abstract":"The replication factor Cdc45 has essential functions in the initiation and elongation steps of eukaryotic DNA<\/jats:styled-content> replication and plays an important role in the intra\u2010S\u2010phase checkpoint. Its interactions with other replication proteins during the cell cycle and after intra\u2010S\u2010phase checkpoint activation are only partially characterized. In the present study, we show that the C terminal part of Cdc45 may mediate its interactions with Claspin. The interactions of human Cdc45 with the three replication factors Claspin, replication protein A and DNA<\/jats:styled-content> polymerase \u03b4 are maximal during the S phase. Following UVC<\/jats:styled-content>\u2010induced DNA<\/jats:styled-content> damage, Cdc45\u2013Claspin complex formation is reduced, whereas the binding of Cdc45 to replication protein A is not affected. We also show that treatment of cells with UCN<\/jats:styled-content>\u201001 and phosphatidylinositol 3\u2010kinase\u2010like kinase inhibitors does not rescue the UV<\/jats:styled-content>\u2010induced destabilization of Cdc45\u2013Claspin interactions, suggesting that the loss of the interaction between Cdc45 and Claspin occurs upstream of ataxia telangiectasia and Rad 3\u2010related activation in the intra\u2010S\u2010phase checkpoint.<\/jats:p><\/jats:sec>Structured digital abstract<\/jats:title>\n\n\nClapsin<\/jats:ext-link> physically interacts<\/jats:ext-link> with Cdc45<\/jats:ext-link> by anti bait coimmunoprecipitation<\/jats:ext-link> (View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n\nCdc45<\/jats:ext-link> physically interacts<\/jats:ext-link> with RPA32<\/jats:ext-link>, Clapsin<\/jats:ext-link> and p125 Pol delta<\/jats:ext-link> by pull down<\/jats:ext-link> (View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n\nCdc45<\/jats:ext-link> physically interacts<\/jats:ext-link> with RPA32<\/jats:ext-link> by pull down<\/jats:ext-link> (View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n\nCdc45<\/jats:ext-link> physically interacts<\/jats:ext-link> with Clapsin<\/jats:ext-link> by pull down<\/jats:ext-link> (View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n\nCdc45<\/jats:ext-link> physically interacts<\/jats:ext-link> with Clapsin<\/jats:ext-link> and RPA32<\/jats:ext-link> by pull down<\/jats:ext-link> (View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n\nRPA32<\/jats:ext-link> physically interacts<\/jats:ext-link> with Cdc45<\/jats:ext-link> by anti bait coimmunoprecipitation<\/jats:ext-link> (View interaction<\/jats:ext-link>)<\/jats:p><\/jats:list-item>\n<\/jats:list>\n<\/jats:p><\/jats:sec>","DOI":"10.1111\/febs.12465","type":"journal-article","created":{"date-parts":[[2013,8,2]],"date-time":"2013-08-02T16:08:38Z","timestamp":1375459718000},"page":"4888-4902","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Cell cycle\u2010dependent formation of Cdc45\u2013Claspin complexes in human cells is compromized by UV<\/scp>\u2010mediated DNA<\/scp> damage"],"prefix":"10.1111","volume":"280","author":[{"given":"Ronan","family":"Broderick","sequence":"first","affiliation":[{"name":"Centre for Chromosome Biology School of Natural Sciences National University of Ireland Galway Ireland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael D.","family":"Rainey","sequence":"additional","affiliation":[{"name":"Centre for Chromosome Biology School of Natural Sciences National University of Ireland 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