Journal
CELL HOST & MICROBE
Volume 11, Issue 5, Pages 528-537Publisher
CELL PRESS
DOI: 10.1016/j.chom.2012.04.006
Keywords
-
Categories
Funding
- NIH [AI060389, AI88778, DA015625, DA024563]
Ask authors/readers for more resources
RIG-I is a cytosolic pathogen recognition receptor that initiates immune responses against RNA viruses. Upon viral RNA recognition, antiviral signaling requires RIG-I redistribution from the cytosol to membranes where it binds the adaptor protein, MAVS. Here we identify the mitochondrial targeting chaperone protein, 14-3-3 epsilon, as a RIG-I-binding partner and essential component of a translocation complex or translocon containing RIG-I, 14-3-3 epsilon, and the TRIM25 ubiquitin ligase. The RIG-I translocon directs RIG-I redistribution from the cytosol to membranes where it mediates MAVS-dependent innate immune signaling during acute RNA virus infection. 14-3-3 epsilon is essential for the stable interaction of RIG-I with TRIM25, which facilitates RIG-I ubiquitination and initiation of innate immunity against hepatitis C virus and other pathogenic RNA viruses. Our results define 14-3-3 epsilon as a key component of a RIG-I translocon required for innate antiviral immunity.
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