SUMOylation of RIG-I positively regulates the type I interferon signaling
Protein & Cell
;
(12): 275-283, 2010.
Article
in English
| WPRIM
| ID: wpr-757728
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Physiology
/
Binding Sites
/
Base Sequence
/
HeLa Cells
/
Signal Transduction
/
Interferon Type I
/
Chemistry
/
DNA Primers
/
Sendai virus
/
SUMO-1 Protein
Limits:
Humans
Language:
English
Journal:
Protein & Cell
Year:
2010
Type:
Article
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