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

Author

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  • Wenshuai Wang

    (Yale University
    Yale University)

  • Benjamin Götte

    (Yale University)

  • Rong Guo

    (Yale University)

  • Anna Marie Pyle

    (Yale University
    Yale University)

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.

Suggested Citation

  • Wenshuai Wang & Benjamin Götte & Rong Guo & Anna Marie Pyle, 2023. "The E3 ligase Riplet promotes RIG-I signaling independent of RIG-I oligomerization," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-42982-0
    DOI: 10.1038/s41467-023-42982-0
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    References listed on IDEAS

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    1. Alys Peisley & Bin Wu & Hui Xu & Zhijian J. Chen & Sun Hur, 2014. "Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I," Nature, Nature, vol. 509(7498), pages 110-114, May.
    2. Yuheng Shi & Bofeng Yuan & Wenting Zhu & Rui Zhang & Lin Li & Xiaojing Hao & She Chen & Fajian Hou, 2017. "Ube2D3 and Ube2N are essential for RIG-I-mediated MAVS aggregation in antiviral innate immunity," Nature Communications, Nature, vol. 8(1), pages 1-14, August.
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