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dc.contributor.author이철주-
dc.contributor.author이은영-
dc.contributor.author이현철-
dc.contributor.author김현권-
dc.contributor.author장송이-
dc.contributor.author박성준-
dc.contributor.author김용훈-
dc.contributor.author김정환-
dc.contributor.author황정원-
dc.contributor.author김재훈-
dc.contributor.author김태환-
dc.contributor.authorAbul Arif-
dc.contributor.author김선영-
dc.contributor.author최영기-
dc.contributor.author이철호-
dc.contributor.author정재유-
dc.contributor.authorPaul L Fox-
dc.contributor.author김성훈-
dc.contributor.author이정수-
dc.contributor.author김명희-
dc.date.accessioned2021-06-09T04:17:08Z-
dc.date.available2021-06-09T04:17:08Z-
dc.date.issued2016-11-
dc.identifier.citationVOL 17, NO 11-1262-
dc.identifier.issn1529-2908-
dc.identifier.other47794-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/65032-
dc.description.abstractThe mammalian cytoplasmic multi-tRNA synthetase complex (MSC) is a depot system that regulates non-translational cellular functions. Here we found that the MSC component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function following viral infection and exhibited potent antiviral activity. Infection-specific phosphorylation of EPRS at Ser990 induced its dissociation from the MSC, after which it was guided to the antiviral signaling pathway, where it interacted with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity. This interaction blocked PCBP2-mediated ubiquitination of MAVS and ultimately suppressed viral replication. EPRS-haploid (Eprs(+/-)) mice showed enhanced viremia and inflammation and delayed viral clearance. This stimulus-inducible activation of MAVS by EPRS suggests an unexpected role for the MSC as a regulator of immune responses to viral infection-
dc.publisherNature immunology-
dc.titleInfection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity-
dc.typeArticle-
dc.relation.page12521262-
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