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http://purl.uniprot.org/citations/27561354http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27561354http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27561354http://www.w3.org/2000/01/rdf-schema#comment"Human CtIP is a decisive factor in DNA double-strand break repair pathway choice by enabling DNA-end resection, the first step that differentiates homologous recombination (HR) from non-homologous end-joining (NHEJ). To coordinate appropriate and timely execution of DNA-end resection, CtIP function is tightly controlled by multiple protein-protein interactions and post-translational modifications. Here, we identify the Cullin3 E3 ligase substrate adaptor Kelch-like protein 15 (KLHL15) as a new interaction partner of CtIP and show that KLHL15 promotes CtIP protein turnover via the ubiquitin-proteasome pathway. A tripeptide motif (FRY) conserved across vertebrate CtIP proteins is essential for KLHL15-binding; its mutation blocks KLHL15-dependent CtIP ubiquitination and degradation. Consequently, DNA-end resection is strongly attenuated in cells overexpressing KLHL15 but amplified in cells either expressing a CtIP-FRY mutant or lacking KLHL15, thus impacting the balance between HR and NHEJ. Collectively, our findings underline the key importance and high complexity of CtIP modulation for genome integrity."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.org/dc/terms/identifier"doi:10.1038/ncomms12628"xsd:string
http://purl.uniprot.org/citations/27561354http://purl.org/dc/terms/identifier"doi:10.1038/ncomms12628"xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Peter M."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Peter M."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Sartori A.A."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Sartori A.A."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Walker C."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Walker C."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Porro A."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Porro A."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Freire R."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Freire R."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Enchev R.I."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Enchev R.I."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Murina O."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Murina O."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Eggenschwiler A."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Eggenschwiler A."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Ferretti L.P."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Ferretti L.P."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Himmels S.F."xsd:string
http://purl.uniprot.org/citations/27561354http://purl.uniprot.org/core/author"Himmels S.F."xsd:string