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The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation

Author

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  • Xuemei Bai

    (Shandong University)

  • Chao Sui

    (Shandong University)

  • Feng Liu

    (Shandong University)

  • Tian Chen

    (Shandong University)

  • Lei Zhang

    (Shandong University)

  • Yi Zheng

    (Shandong University)

  • Bingyu Liu

    (Shandong University)

  • Chengjiang Gao

    (Shandong University)

Abstract

The signaling adaptor MAVS forms prion-like aggregates to activate the innate antiviral immune response after viral infection. However, spontaneous aggregation of MAVS can lead to autoimmune diseases. The molecular mechanism that prevents MAVS from spontaneous aggregation in resting cells has been enigmatic. Here we report that protein arginine methyltransferase 9 targets MAVS directly and catalyzes the arginine methylation of MAVS at the Arg41 and Arg43. In the resting state, this modification inhibits MAVS aggregation and autoactivation of MAVS. Upon virus infection, PRMT9 dissociates from the mitochondria, leading to the aggregation and activation of MAVS. Our study implicates a form of post-translational modification on MAVS, which can keep MAVS inactive in physiological conditions to maintain innate immune homeostasis.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32628-y
    DOI: 10.1038/s41467-022-32628-y
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    1. Jiaxin Li & Rui Zhang & Changwan Wang & Junyan Zhu & Miao Ren & Yingbo Jiang & Xianteng Hou & Yangting Du & Qing Wu & Shishi Qi & Lin Li & She Chen & Hui Yang & Fajian Hou, 2023. "WDR77 inhibits prion-like aggregation of MAVS to limit antiviral innate immune response," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. Lei Shen & Xiaokuang Ma & Yuanyuan Wang & Zhihao Wang & Yi Zhang & Hoang Quoc Hai Pham & Xiaoqun Tao & Yuehua Cui & Jing Wei & Dimitri Lin & Tharindumala Abeywanada & Swanand Hardikar & Levon Halabeli, 2024. "Loss-of-function mutation in PRMT9 causes abnormal synapse development by dysregulation of RNA alternative splicing," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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