The E3 ligase Riplet promotes RIG-I signaling independent of RIG-I oligomerization

Wenshuai Wang, Benjamin Götte, Rong Guo and Anna Marie Pyle ()
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Wenshuai Wang: Yale University
Benjamin Götte: Yale University
Rong Guo: Yale University
Anna Marie Pyle: Yale University

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: Abstract RIG-I is an essential innate immune receptor that responds to infection by RNA viruses. The RIG-I signaling cascade is mediated by a series of post-translational modifications, the most important of which is ubiquitination of the RIG-I Caspase Recruitment Domains (CARDs) by E3 ligase Riplet. This is required for interaction between RIG-I and its downstream adapter protein MAVS, but the mechanism of action remains unclear. Here we show that Riplet is required for RIG-I signaling in the presence of both short and long dsRNAs, establishing that Riplet activation does not depend upon RIG-I filament formation on long dsRNAs. Likewise, quantitative Riplet-RIG-I affinity measurements establish that Riplet interacts with RIG-I regardless of whether the receptor is bound to RNA. To understand this, we solved high-resolution cryo-EM structures of RIG-I/RNA/Riplet complexes, revealing molecular interfaces that control Riplet-mediated activation and enabling the formulation of a unified model for the role of Riplet in signaling.

Date: 2023
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DOI: 10.1038/s41467-023-42982-0

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