UXT-V1 facilitates the formation of MAVS antiviral signalosome on mitochondria.

Yuefeng Huang, Heng Liu, Rui Ge, Yi Zhou, Xiwen Lou, Chen Wang

Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.

Journal of immunology (Baltimore, Md. : 1950) 2012 Jan 1

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Virus infection induces the MAVS-TNFR-associated factor (TRAF) 3 signaling axis on mitochondria. It remains to elucidate the corresponding regulatory processes. In this study, we identify UXT-V1 as a novel TRAF3-binding protein. UXT-V1 is critical for the virus-induced activation of NF-κB and IFN regulatory factor 3. Reduction of UXT-V1 impairs the induction of IFN-β and attenuates the host antiviral responses. The N-terminal TRAF-binding motif of UXT-V1 binds to the C-terminal TRAF domain of TRAF3, thus facilitating the interaction between TRAF3 and MAVS. Notably, TRAF3 and TNFR-associated death domain protein are recruited onto mitochondria upon virus infection. These translocations are blocked when knocking down UXT-V1. Thus, UXT-V1 represents a novel integral component of the MAVS signalosome on mitochondria, mediating the innate antiviral signal transduction.

Citation

Yuefeng Huang, Heng Liu, Rui Ge, Yi Zhou, Xiwen Lou, Chen Wang. UXT-V1 facilitates the formation of MAVS antiviral signalosome on mitochondria. Journal of immunology (Baltimore, Md. : 1950). 2012 Jan 1;188(1):358-66