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

Title
Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity
Authors
이철주이은영이현철김현권장송이박성준김용훈김정환황정원김재훈김태환Abul Arif김선영최영기이철호정재유Paul L Fox김성훈이정수김명희
Issue Date
2016-11
Publisher
Nature immunology
Citation
VOL 17, NO 11-1262
Abstract
The 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
URI
http://pubs.kist.re.kr/handle/201004/65032
ISSN
1529-2908
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KIST Publication > Article
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