SUMOylation of RIG-I positively regulates the type I interferon signaling.
10.1007/s13238-010-0030-1
- Author:
Zhiqiang MI
1
;
Jihuan FU
;
Yanbao XIONG
;
Hong TANG
Author Information
1. Center for Molecular Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
- Publication Type:Journal Article
- MeSH:
Adaptor Proteins, Signal Transducing;
physiology;
Base Sequence;
Binding Sites;
DEAD Box Protein 58;
DEAD-box RNA Helicases;
chemistry;
genetics;
immunology;
physiology;
DNA Primers;
genetics;
Gene Knockdown Techniques;
HEK293 Cells;
HeLa Cells;
Humans;
Immunity, Innate;
Interferon Type I;
immunology;
physiology;
RNA Interference;
SUMO-1 Protein;
physiology;
Sendai virus;
immunology;
Signal Transduction;
Sumoylation;
Ubiquitin-Conjugating Enzymes;
antagonists & inhibitors;
genetics;
physiology
- From:
Protein & Cell
2010;1(3):275-283
- CountryChina
- Language:English
-
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.
