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http://purl.uniprot.org/citations/23045548http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23045548http://www.w3.org/2000/01/rdf-schema#comment"The WD40-repeat protein DDB2 is essential for efficient recognition and subsequent removal of ultraviolet (UV)-induced DNA lesions by nucleotide excision repair (NER). However, how DDB2 promotes NER in chromatin is poorly understood. Here, we identify poly(ADP-ribose) polymerase 1 (PARP1) as a novel DDB2-associated factor. We demonstrate that DDB2 facilitated poly(ADP-ribosyl)ation of UV-damaged chromatin through the activity of PARP1, resulting in the recruitment of the chromatin-remodeling enzyme ALC1. Depletion of ALC1 rendered cells sensitive to UV and impaired repair of UV-induced DNA lesions. Additionally, DDB2 itself was targeted by poly(ADP-ribosyl)ation, resulting in increased protein stability and a prolonged chromatin retention time. Our in vitro and in vivo data support a model in which poly(ADP-ribosyl)ation of DDB2 suppresses DDB2 ubiquitylation and outline a molecular mechanism for PARP1-mediated regulation of NER through DDB2 stabilization and recruitment of the chromatin remodeler ALC1."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.org/dc/terms/identifier"doi:10.1083/jcb.201112132"xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Vermeulen W."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Matsumoto S."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"de Groot A."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Deelder A."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Pines A."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Marteijn J.A."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Typas D."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Vrieling H."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Sugasawa K."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Luijsterburg M.S."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Hensbergen P."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Thoma N."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Vrouwe M.G."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Cansoy M."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/author"Mullenders L."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/name"J Cell Biol"xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/pages"235-249"xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/title"PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1."xsd:string
http://purl.uniprot.org/citations/23045548http://purl.uniprot.org/core/volume"199"xsd:string
http://purl.uniprot.org/citations/23045548http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23045548
http://purl.uniprot.org/citations/23045548http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23045548