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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing / physiology
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Base Sequence
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Binding Sites
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DEAD Box Protein 58
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DEAD-box RNA Helicases / chemistry
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DEAD-box RNA Helicases / genetics
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DEAD-box RNA Helicases / immunology
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DEAD-box RNA Helicases / physiology*
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DNA Primers / genetics
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Gene Knockdown Techniques
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HEK293 Cells
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HeLa Cells
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Humans
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Immunity, Innate
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Interferon Type I / immunology
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Interferon Type I / physiology*
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RNA Interference
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Receptors, Immunologic
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SUMO-1 Protein / physiology
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Sendai virus / immunology
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Signal Transduction
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Sumoylation
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Ubiquitin-Conjugating Enzymes / antagonists & inhibitors
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Ubiquitin-Conjugating Enzymes / genetics
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Ubiquitin-Conjugating Enzymes / physiology
Substances
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Adaptor Proteins, Signal Transducing
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DNA Primers
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Interferon Type I
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MAVS protein, human
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Receptors, Immunologic
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SUMO-1 Protein
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SUMO1 protein, human
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Ubiquitin-Conjugating Enzymes
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RIGI protein, human
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DEAD Box Protein 58
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DEAD-box RNA Helicases
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ubiquitin-conjugating enzyme UBC9