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;
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History+
Published Online
2010-03-01
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(276KB)
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.
Zhiqiang Mi, Jihuan Fu, Yanbao Xiong, Hong Tang,.
SUMOylation of RIG-I positively regulates the
type I interferon signaling.
Protein Cell, 2010, 1(3): 275-283 DOI:10.1007/s13238-010-0030-1
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(276KB)
