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USP18 positively regulates innate antiviral immunity by promoting K63-linked polyubiquitination of MAVS

Author

Listed:
  • Jinxiu Hou

    (Shandong University)

  • Lulu Han

    (Shandong University)

  • Ze Zhao

    (Shandong University)

  • Huiqing Liu

    (Shandong University)

  • Lei Zhang

    (Shandong University)

  • Chunhong Ma

    (Shandong University)

  • Fan Yi

    (Shandong University)

  • Bingyu Liu

    (Shandong University)

  • Yi Zheng

    (Shandong University)

  • Chengjiang Gao

    (Shandong University)

Abstract

Activation of MAVS, an adaptor molecule in Rig-I-like receptor (RLR) signaling, is indispensable for antiviral immunity, yet the molecular mechanisms modulating MAVS activation are not completely understood. Ubiquitination has a central function in regulating the activity of MAVS. Here, we demonstrate that a mitochondria-localized deubiquitinase USP18 specifically interacts with MAVS, promotes K63-linked polyubiquitination and subsequent aggregation of MAVS. USP18 upregulates the expression and production of type I interferon following infection with Sendai virus (SeV) or Encephalomyocarditis virus (EMCV). Mice with a deficiency of USP18 are more susceptible to RNA virus infection. USP18 functions as a scaffold protein to facilitate the re-localization of TRIM31 and enhances the interaction between TRIM31 and MAVS in mitochondria. Our results indicate that USP18 functions as a post-translational modulator of MAVS-mediated antiviral signaling.

Suggested Citation

  • Jinxiu Hou & Lulu Han & Ze Zhao & Huiqing Liu & Lei Zhang & Chunhong Ma & Fan Yi & Bingyu Liu & Yi Zheng & Chengjiang Gao, 2021. "USP18 positively regulates innate antiviral immunity by promoting K63-linked polyubiquitination of MAVS," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23219-4
    DOI: 10.1038/s41467-021-23219-4
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    Cited by:

    1. Xuemei Bai & Chao Sui & Feng Liu & Tian Chen & Lei Zhang & Yi Zheng & Bingyu Liu & Chengjiang Gao, 2022. "The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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