You are here
The mitochondrial targeting chaperone 14-3-3ε regulates a RIG-I translocon that mediates membrane association and innate antiviral immunity.
| Title | The mitochondrial targeting chaperone 14-3-3ε regulates a RIG-I translocon that mediates membrane association and innate antiviral immunity. |
| Publication Type | Journal Article |
| Year of Publication | 2012 |
| Authors | Liu, HMinyi, Loo, Y-M, Horner, SM, Zornetzer, GA, Katze, MG, Gale, M |
| Journal | Cell Host Microbe |
| Volume | 11 |
| Issue | 5 |
| Pagination | 528-37 |
| Date Published | 2012 May 17 |
| ISSN | 1934-6069 |
| Keywords | 14-3-3 Proteins, Antiviral Agents, Cell Line, DEAD-box RNA Helicases, Hepacivirus, Humans, Membrane Proteins, Models, Biological, Molecular Chaperones, Protein Binding, Protein Interaction Mapping, Transcription Factors, Ubiquitin-Protein Ligases |
| Abstract | 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, 14-3-3ε, as a RIG-I-binding partner and essential component of a translocation complex or "translocon" containing RIG-I, 14-3-3ε, 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. 14-3-3ε 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 14-3-3ε as a key component of a RIG-I translocon required for innate antiviral immunity. |
| DOI | 10.1016/j.chom.2012.04.006 |
| Alternate Journal | Cell Host Microbe |
| PubMed ID | 22607805 |
