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http://purl.uniprot.org/citations/25865883http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25865883http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25865883http://www.w3.org/2000/01/rdf-schema#comment"MDA5 is a cytoplasmic viral double-stranded RNA (dsRNA) sensor and triggers type I interferon (IFN) production. MDA5 assembles along viral dsRNA, leading to the formation of an MDA5 filament required for activating the MAVS adaptor. A recent study has revealed that PP1α and PP1γ phosphatases are responsible for dephosphorylating MDA5 and are essential for its activation. Here, we identified RIO kinase 3 (RIOK3) as a protein kinase that phosphorylates the MDA5 C-terminal region. RIOK3 knockout strongly enhanced type I IFN and IFN-inducible gene expression following measles virus infection. Conversely, the ectopic expression of RIOK3 or a phosphomimetic MDA5-S828D mutation attenuated MDA5-mediated signaling. Moreover, RIOK3-mediated MDA5 phosphorylation impaired MDA5 multimer formation, indicating that MDA5 C-terminal phosphorylation interferes with MDA5 filament formation and suppresses its signaling. Our data revealed a regulatory mechanism underlying the activation of the cytoplasmic viral RNA sensor MDA5 in both uninfected and virus-infected cells."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2015.03.027"xsd:string
http://purl.uniprot.org/citations/25865883http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2015.03.027"xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/author"Matsumoto M."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/author"Matsumoto M."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/author"Takashima K."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/author"Takashima K."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/author"Seya T."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/author"Seya T."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/author"Oshiumi H."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/author"Oshiumi H."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/author"Takaki H."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/author"Takaki H."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/pages"192-200"xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/pages"192-200"xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/title"RIOK3-mediated phosphorylation of MDA5 interferes with its assembly and attenuates the innate immune response."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/title"RIOK3-mediated phosphorylation of MDA5 interferes with its assembly and attenuates the innate immune response."xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/25865883http://purl.uniprot.org/core/volume"11"xsd:string