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http://purl.uniprot.org/citations/28436945http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28436945http://www.w3.org/2000/01/rdf-schema#comment"Both p150 and p110 isoforms of ADAR1 convert adenosine to inosine in double-stranded RNA (dsRNA). ADAR1p150 suppresses the dsRNA-sensing mechanism that activates MDA5-MAVS-IFN signaling in the cytoplasm. In contrast, the biological function of the ADAR1p110 isoform, which is usually located in the nucleus, is largely unknown. Here, we show that stress-activated phosphorylation of ADAR1p110 by MKK6-p38-MSK MAP kinases promotes its binding to Exportin-5 and its export from the nucleus. After translocating to the cytoplasm, ADAR1p110 suppresses apoptosis in stressed cells by protecting many antiapoptotic gene transcripts that contain 3'-untranslated-region dsRNA structures primarily comprising inverted Alu repeats. ADAR1p110 competitively inhibits binding of Staufen1 to the 3'-untranslated-region dsRNAs and antagonizes Staufen1-mediated mRNA decay. Our study reveals a new stress-response mechanism in which human ADAR1p110 and Staufen1 regulate surveillance of a set of mRNAs required for survival of stressed cells."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.3403"xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Song C."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Sakurai M."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Speicher D.W."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Skordalakes E."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Nishikura K."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Ota H."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Showe L.C."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Tang H.Y."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Shiromoto Y."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Kossenkov A.V."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/author"Wickramasinghe J."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/pages"534-543"xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/title"ADAR1 controls apoptosis of stressed cells by inhibiting Staufen1-mediated mRNA decay."xsd:string
http://purl.uniprot.org/citations/28436945http://purl.uniprot.org/core/volume"24"xsd:string
http://purl.uniprot.org/citations/28436945http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28436945
http://purl.uniprot.org/citations/28436945http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28436945
http://purl.uniprot.org/uniprot/#_A0A024DAK3-mappedCitation-28436945http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28436945
http://purl.uniprot.org/uniprot/#_A2IBT1-mappedCitation-28436945http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28436945
http://purl.uniprot.org/uniprot/#_A2IBT2-mappedCitation-28436945http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28436945
http://purl.uniprot.org/uniprot/#_B3KRE0-mappedCitation-28436945http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28436945