http://purl.uniprot.org/citations/28436945 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/28436945 | http://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/28436945 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsmb.3403"xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Song C."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Sakurai M."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Speicher D.W."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Skordalakes E."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Nishikura K."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Ota H."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Showe L.C."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Tang H.Y."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Shiromoto Y."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Kossenkov A.V."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/author | "Wickramasinghe J."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/name | "Nat Struct Mol Biol"xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/pages | "534-543"xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/title | "ADAR1 controls apoptosis of stressed cells by inhibiting Staufen1-mediated mRNA decay."xsd:string |
http://purl.uniprot.org/citations/28436945 | http://purl.uniprot.org/core/volume | "24"xsd:string |
http://purl.uniprot.org/citations/28436945 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/28436945 |
http://purl.uniprot.org/citations/28436945 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/28436945 |
http://purl.uniprot.org/uniprot/#_A0A024DAK3-mappedCitation-28436945 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28436945 |
http://purl.uniprot.org/uniprot/#_A2IBT1-mappedCitation-28436945 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28436945 |
http://purl.uniprot.org/uniprot/#_A2IBT2-mappedCitation-28436945 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28436945 |
http://purl.uniprot.org/uniprot/#_B3KRE0-mappedCitation-28436945 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/28436945 |