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Title 

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

Authors 

Eun Young LeeH C LeeHyun-Kwan KimSong Yee JangS J ParkYong-Hoon KimJong Hwan KimJungwon HwangJ H KimT H KimA ArifSeon-Young KimY K ChoiC LeeChul Ho LeeJ U JungP L FoxS KimJ S LeeMyung Hee Kim

Publisher 

Nature Publishing Group

Issue Date 

2016

Citation 

Nature Immunology, vol. 17, no. 11, pp. 1252-1262

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.

ISSN 

1529-2908

Link 

http://dx.doi.org/10.1038/ni.3542

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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