Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity

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dc.contributor.authorEun Young Lee-
dc.contributor.authorH C Lee-
dc.contributor.authorHyun-Kwan Kim-
dc.contributor.authorSong Yee Jang-
dc.contributor.authorS J Park-
dc.contributor.authorYong-Hoon Kim-
dc.contributor.authorJong Hwan Kim-
dc.contributor.authorJungwon Hwang-
dc.contributor.authorJ H Kim-
dc.contributor.authorT H Kim-
dc.contributor.authorA Arif-
dc.contributor.authorSeon-Young Kim-
dc.contributor.authorY K Choi-
dc.contributor.authorC Lee-
dc.contributor.authorChul Ho Lee-
dc.contributor.authorJ U Jung-
dc.contributor.authorP L Fox-
dc.contributor.authorS Kim-
dc.contributor.authorJ S Lee-
dc.contributor.authorMyung Hee Kim-
dc.date.accessioned2017-04-19T10:28:05Z-
dc.date.available2017-04-19T10:28:05Z-
dc.date.issued2016-
dc.identifier.issn1529-2908-
dc.identifier.uri10.1038/ni.3542ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13466-
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.publisherSpringer-Nature Pub Group-
dc.titleInfection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity-
dc.title.alternativeInfection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity-
dc.typeArticle-
dc.citation.titleNature Immunology-
dc.citation.number11-
dc.citation.endPage1262-
dc.citation.startPage1252-
dc.citation.volume17-
dc.contributor.affiliatedAuthorEun Young Lee-
dc.contributor.affiliatedAuthorHyun-Kwan Kim-
dc.contributor.affiliatedAuthorSong Yee Jang-
dc.contributor.affiliatedAuthorYong-Hoon Kim-
dc.contributor.affiliatedAuthorJong Hwan Kim-
dc.contributor.affiliatedAuthorJungwon Hwang-
dc.contributor.affiliatedAuthorSeon-Young Kim-
dc.contributor.affiliatedAuthorChul Ho Lee-
dc.contributor.affiliatedAuthorMyung Hee Kim-
dc.contributor.alternativeName이은영-
dc.contributor.alternativeName이현철-
dc.contributor.alternativeName김현관-
dc.contributor.alternativeName장송이-
dc.contributor.alternativeName박성준-
dc.contributor.alternativeName김용훈-
dc.contributor.alternativeName김종환-
dc.contributor.alternativeName황중원-
dc.contributor.alternativeName김재훈-
dc.contributor.alternativeName김태환-
dc.contributor.alternativeNameArif-
dc.contributor.alternativeName김선영-
dc.contributor.alternativeName최영기-
dc.contributor.alternativeName이철주-
dc.contributor.alternativeName이철호-
dc.contributor.alternativeName정재웅-
dc.contributor.alternativeNameFox-
dc.contributor.alternativeName김성훈-
dc.contributor.alternativeName이종수-
dc.contributor.alternativeName김명희-
dc.identifier.bibliographicCitationNature Immunology, vol. 17, no. 11, pp. 1252-1262-
dc.identifier.doi10.1038/ni.3542-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
Ochang Branch Institute > Division of National Bio-Infrastructure > Laboratory Animal Resource & Research Center > 1. Journal Articles
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