RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/25210797http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25210797http://www.w3.org/2000/01/rdf-schema#comment"Che-1/AATF is an RNA polymerase II-binding protein that is involved in the regulation of gene transcription, which undergoes stabilization and accumulation in response to DNA damage. We have previously demonstrated that following apoptotic induction, Che-1 protein levels are downregulated through its interaction with the E3 ligase HDM2, which leads to Che-1 degradation by ubiquitylation. This interaction is mediated by Pin1, which determines a phosphorylation-dependent conformational change. Here we demonstrate that HIPK2, a proapoptotic kinase, is involved in Che-1 degradation. HIPK2 interacts with Che-1 and, upon genotoxic stress, phosphorylates it at specific residues. This event strongly increases HDM2/Che-1 interaction and degradation of Che-1 protein via ubiquitin-dependent proteasomal system. In agreement with these findings, we found that HIPK2 depletion strongly decreases Che-1 ubiquitylation and degradation. Notably, Che-1 overexpression strongly counteracts HIPK2-induced apoptosis. Our results establish Che-1 as a new HIPK2 target and confirm its important role in the cellular response to DNA damage."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.org/dc/terms/identifier"doi:10.1038/cddis.2014.381"xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Camerini S."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Crescenzi M."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Bruno T."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"De Nicola F."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Fanciulli M."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Floridi A."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Iezzi S."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Passananti C."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Soddu S."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Rinaldo C."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Desantis A."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Sorino C."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/author"Catena V."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/name"Cell Death Dis"xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/pages"e1414"xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/title"HIPK2 sustains apoptotic response by phosphorylating Che-1/AATF and promoting its degradation."xsd:string
http://purl.uniprot.org/citations/25210797http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/25210797http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25210797
http://purl.uniprot.org/citations/25210797http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25210797
http://purl.uniprot.org/uniprot/#_A4D1R9-mappedCitation-25210797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25210797
http://purl.uniprot.org/uniprot/#_Q9H2X6-mappedCitation-25210797http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25210797