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http://purl.uniprot.org/citations/23623683http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23623683http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23623683http://www.w3.org/2000/01/rdf-schema#comment"The regulation of DNA double-strand break (DSB) repair by phosphorylation-dependent signaling pathways is crucial for the maintenance of genome stability; however, remarkably little is known about the molecular mechanisms by which phosphorylation controls DSB repair. Here, we show that PIN1, a phosphorylation-specific prolyl isomerase, interacts with key DSB repair factors and affects the relative contributions of homologous recombination (HR) and nonhomologous end-joining (NHEJ) to DSB repair. We find that PIN1-deficient cells display reduced NHEJ due to increased DNA end resection, whereas resection and HR are compromised in PIN1-overexpressing cells. Moreover, we identify CtIP as a substrate of PIN1 and show that DSBs become hyperresected in cells expressing a CtIP mutant refractory to PIN1 recognition. Mechanistically, we provide evidence that PIN1 impinges on CtIP stability by promoting its ubiquitylation and subsequent proteasomal degradation. Collectively, these data uncover PIN1-mediated isomerization as a regulatory mechanism coordinating DSB repair."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2013.03.023"xsd:string
http://purl.uniprot.org/citations/23623683http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2013.03.023"xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Gerrits B."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Gerrits B."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Sartori A.A."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Sartori A.A."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Steger M."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Steger M."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Zerbe O."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Zerbe O."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Janscak P."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Janscak P."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Del Sal G."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Del Sal G."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Murina O."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Murina O."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Ferretti L.P."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Ferretti L.P."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Haenggi K."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Haenggi K."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Huehn D."xsd:string
http://purl.uniprot.org/citations/23623683http://purl.uniprot.org/core/author"Huehn D."xsd:string