Journal
PROTEIN & CELL
Volume 1, Issue 3, Pages 275-283Publisher
HIGHER EDUCATION PRESS
DOI: 10.1007/s13238-010-0030-1
Keywords
RIG-I; SUMOylation; type I interferon; innate immunity
Categories
Funding
- Chinese Academy of Sciences [KSCX1-YW-10]
- Ministry of Science and Technology [2006CB910901, 2007DFC30190, 2008ZX10001-002, 2009CB522506]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available