Journal
MOLECULAR CELL
Volume 68, Issue 2, Pages 293-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2017.09.035
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Funding
- NCI, NIH [R01CA101795]
- Cancer Prevention and Research Institute of Texas (CPRIT) [RP121048]
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Mitochondrial antiviral signaling platform protein (MAVS) acts as a central hub for RIG-I receptor proximal signal propagation. However, key components in the assembly of the MAVS mitochondrial platform that promote RIG-I mitochondrial localization and optimal activation are still largely undefined. Employing pooled RNAi and yeast two-hybrid screenings, we report that the mitochondrial adaptor protein tripartite motif (TRIM) 14 provides a docking platform for the assembly of the mitochondrial signaling complex required for maximal activation of RIGI-mediated signaling, consisting of WHIP and protein phosphatase PPP6C. Following viral infection, the ubiquitin-binding domain in WHIP bridges RIG-I with MAVS by binding to polyUb chains of RIG-I at lysine 164. The ATPase domain in WHIP contributes to stabilization of the RIG-I-dsRNA interaction. Moreover, phosphatase PPP6C is responsible for RIG-I dephosphorylation. Together, our findings define the WHIP-TRIM14-PPP6C mitochondrial signalosome required for RIG-I-mediated innate antiviral immunity.
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