Research articles

SUMOylation of RIG-I positively regulates the type I interferon signaling

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  • 1.Center for Molecular Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China;Key Laboratory of Infection and Immunity of Chinese Academy of Sciences, Institute of Biophysics, Beijing 100101, China; 2.Key Laboratory of Infection and Immunity of Chinese Academy of Sciences, Institute of Biophysics, Beijing 100101, China;

Published date: 01 Mar 2010

Abstract

Retinoic acid-inducible gene-I (RIG-I) functions as an intracellular pattern recognition receptor (PRR) that recognizes the 5’-triphosphate moiety of single-stranded RNA viruses to initiate the innate immune response. Previous studies have shown that Lys63-linked ubiquitylation is required for RIG-I activation and the downstream anti-viral type I interferon (IFN-I) induction. Herein we reported that, RIG-I was also modified by small ubiquitin-like modifier-1 (SUMO-1). Functional analysis showed that RIG-I SUMOylation enhanced IFN-I production through increased ubiquitylation and the interaction with its downstream adaptor molecule Cardif. Our results therefore suggested that SUMOylation might serve as an additional regulatory tier for RIG-I activation and IFN-I signaling.

Cite this article

Zhiqiang Mi, Jihuan Fu, Yanbao Xiong, Hong Tang, . SUMOylation of RIG-I positively regulates the type I interferon signaling[J]. Protein & Cell, 2010 , 1(3) : 275 -283 . DOI: 10.1007/s13238-010-0030-1

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