SUMOylation of RIG-I positively regulates the type I interferon signaling.
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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Base Sequence, Binding Sites, DEAD-box RNA Helicases, DNA Primers, Gene Knockdown Techniques, HEK293 Cells, Hela Cells, Humans, Immunity, Innate, Interferon Type I, RNA Interference, SUMO-1 Protein, Sendai virus, Signal Transduction, Sumoylation, Ubiquitin-Conjugating Enzymes
Adaptor Proteins, Signal Transducing, Base Sequence, Binding Sites, DEAD-box RNA Helicases, DNA Primers, Gene Knockdown Techniques, HEK293 Cells, Hela Cells, Humans, Immunity, Innate, Interferon Type I, RNA Interference, SUMO-1 Protein, Sendai virus, Signal Transduction, Sumoylation, Ubiquitin-Conjugating Enzymes
Protein Cell
Date: Mar. 01, 2010
PubMed ID: 21203974
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