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

Center for Molecular Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Protein & Cell (Impact Factor: 3.25). 03/2010; 1(3):275-83. DOI: 10.1007/s13238-010-0030-1
Source: PubMed


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.

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Available from: Hong Tang
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    • "The innate response is triggered by recognition of pathogen-specific molecules by the Toll-like receptor (TLR) system which then initiates a signaling cascade that activates IRFs 3, 5, and 7 via phosphorylation; the activated IRFs turn on interferon transcription. Two of the TLRs, RIG-1 [47] and MDA5 [48], and an adaptor protein in the TLR signaling pathway known as Pellino-1 [49] have recently been shown to be sumoylated proteins. Sumoylation of RIG-1 enhanced its association with Cardif and led to increased expression of interferon β. "
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    • "Further study indicates that S8 and T170 of RIG-I are two other phosphorylation sites to keep RIG-I latent (Gack et al., 2010; NistalVillán et al., 2010). In addition to ubiquitylation and phosphorylation, recent study reports that RIG-I is also modified by small ubiquitin-like modifier-1 (SUMO-1), which enhances type I IFN production (Mi et al., 2010). "
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