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http://purl.uniprot.org/citations/17468107http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17468107http://www.w3.org/2000/01/rdf-schema#comment"We have previously demonstrated that DNA damage leads to stabilization and accumulation of Che-1, an RNA polymerase II-binding protein that plays an important role in transcriptional activation of p53 and in maintenance of the G(2)/M checkpoint. Here we show that Che-1 is down-regulated during the apoptotic process. We found that the E3 ligase HMD2 physically and functionally interacts with Che-1 and promotes its degradation via the ubiquitin-dependent proteasomal system. Furthermore, we found that in response to apoptotic stimuli Che-1 interacts with the peptidyl-prolyl isomerase Pin1 and that conformational changes generated by Pin1 are required for Che-1/HDM2 interaction. Notably, a Che-1 mutant lacking the capacity to bind Pin1 exhibits an increased half-life and this correlates with a diminished apoptosis in response to genotoxic stress. Our results establish Che-1 as a new Pin1 and HDM2 target and confirm its important role in the cellular response to DNA damage."xsd:string
http://purl.uniprot.org/citations/17468107http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m610282200"xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/author"Bruno T."xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/author"De Nicola F."xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/author"Di Padova M."xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/author"Fanciulli M."xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/author"Floridi A."xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/author"Iezzi S."xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/author"Passananti C."xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/author"Del Sal G."xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/pages"19685-19691"xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/title"The prolyl isomerase Pin1 affects Che-1 stability in response to apoptotic DNA damage."xsd:string
http://purl.uniprot.org/citations/17468107http://purl.uniprot.org/core/volume"282"xsd:string
http://purl.uniprot.org/citations/17468107http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17468107
http://purl.uniprot.org/citations/17468107http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17468107
http://purl.uniprot.org/uniprot/#_B3KUM4-mappedCitation-17468107http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17468107
http://purl.uniprot.org/uniprot/#_P23804-mappedCitation-17468107http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17468107
http://purl.uniprot.org/uniprot/#_Q13526-mappedCitation-17468107http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17468107
http://purl.uniprot.org/uniprot/#_Q2L9A9-mappedCitation-17468107http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17468107
http://purl.uniprot.org/uniprot/#_Q3TVL4-mappedCitation-17468107http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17468107
http://purl.uniprot.org/uniprot/#_Q569X0-mappedCitation-17468107http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17468107
http://purl.uniprot.org/uniprot/#_Q3UTI7-mappedCitation-17468107http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17468107