Research ArticleImmunology

Mitofusin 2 Inhibits Mitochondrial Antiviral Signaling

Sci. Signal.  18 Aug 2009:
Vol. 2, Issue 84, pp. ra47
DOI: 10.1126/scisignal.2000287

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Fusing Roles

Cells use a number of different receptors to detect and respond to various pathogen-associated molecular patterns. For the detection of cytosolic viruses, cells use retinoic acid–inducible gene I (RIG-I) and melanoma differentiation–associated gene 5 (MDA-5), two sensors of viral RNA. Upon binding to nucleic acid, these molecules bind to the adaptor protein MAVS, which is localized at the outer membrane of the mitochondrion. This interaction leads to the production of type I interferon (IFN) as part of the innate immune response to the virus. Yasukawa et al. searched for other outer mitochondrial membrane proteins that might modulate this response and found that mitofusin 2, a guanosine triphosphatase well-characterized for its role in mediating mitochondrial fusion, bound to MAVS and inhibited the activation of the transcription factors needed to trigger the production of IFN. Together, these data suggest that mitofusin 2 acts as an endogenous inhibitor of the antiviral response by inhibiting the interaction between MAVS and either RIG-I or MDA-5.

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