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http://purl.uniprot.org/citations/23159851http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23159851http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23159851http://www.w3.org/2000/01/rdf-schema#comment"Damage-specific DNA-binding protein 2 (DDB2) was first isolated as a subunit of the UV-DDB heterodimeric complex that is involved in DNA damage recognition in the nucleotide excision repair pathway (NER). DDB2 is required for efficient repair of CPDs in chromatin and is a component of the CRL4 (DDB2) E3 ligase that targets XPC, histones and DDB2 itself for ubiquitination. In this study, a yeast two-hybrid screening of a human cDNA library was performed to identify potential DDB2 cellular partners. We identified a deubiquitinating enzyme, USP24, as a likely DDB2-interacting partner. Interaction between DDB2 and USP24 was confirmed by co-precipitation. Importantly, knockdown of USP24 in two human cell lines decreased the steady-state levels of DDB2, indicating that USP24-mediated DDB2 deubiquitination prevents DDB2 degradation. In addition, we demonstrated that USP24 can cleave an ubiquitinated form of DDB2 in vitro. Taken together, our results suggest that the ubiquitin-specific protease USP24 is a novel regulator of DDB2 stability."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.org/dc/terms/identifier"doi:10.4161/cc.22688"xsd:string
http://purl.uniprot.org/citations/23159851http://purl.org/dc/terms/identifier"doi:10.4161/cc.22688"xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/author"Chen H."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/author"Chen H."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/author"Gong F."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/author"Gong F."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/author"Sun Z."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/author"Sun Z."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/author"Zhang L."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/author"Zhang L."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/author"Lubin A."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/author"Lubin A."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/name"Cell Cycle"xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/name"Cell Cycle"xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/pages"4378-4384"xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/pages"4378-4384"xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/title"The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stability."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/title"The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stability."xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/23159851http://purl.uniprot.org/core/volume"11"xsd:string