RIG-I is a cytosolic sensor of RNA viruses. In The EMBO Journal, Lee and colleagues show that deacetylation of the carboxy-terminal region of RIG-I by the cytoplasmic histone deacetylase HDAC6 regulates its RNA-sensing activity. HDAC6-deficient mice are more susceptible to infection with vesicular stomatitis virus, and HDAC6-deficient mouse bone marrow–derived macrophages and embryonic fibroblasts have diminished activation of the type 1 interferon pathway in response to RNA viruses. HDAC6 transiently interacts with RIG-I after viral infection and deacetylates Lys909 of RIG-I. This modification modulates the binding of RIG-I to 5′-triphosphate double-stranded RNA, the activation of type 1 interferon pathways and antiviral responses. These results indicate that acetylation is an additional post-translational modification that can regulate RIG-I function, along with phosphorylation, ubiquitination and sumoylation.
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Visan, I. Deacetylation for viral sensing. Nat Immunol 17, 229 (2016). https://doi.org/10.1038/ni.3406
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DOI: https://doi.org/10.1038/ni.3406
