2. Academic Validation
  3. Arginine monomethylation by PRMT7 controls MAVS-mediated antiviral innate immunity

Arginine monomethylation by PRMT7 controls MAVS-mediated antiviral innate immunity

  • Mol Cell. 2021 Aug 5;81(15):3171-3186.e8. doi: 10.1016/j.molcel.2021.06.004.
Junji Zhu 1,  Xiong Li 1,  Xiaolian Cai 1,  Huangyuan Zha 2,  Ziwen Zhou 1,  Xueyi Sun 1,  Fangjing Rong 1,  Jinghua Tang 1,  Chunchun Zhu 1,  Xing Liu 3,  Sijia Fan 1,  Jing Wang 3,  Qian Liao 1,  Gang Ouyang 3,  Wuhan Xiao 4
Affiliations

Affiliations

  • 1 State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, P.R. China; University of Chinese Academy of Sciences, Beijing 100049, P.R. China.
  • 2 State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, P.R. China.
  • 3 State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, P.R. China; The Key Laboratory of Aquaculture Disease Control, Ministry of Agriculture, Wuhan 430072, P.R. China; The Innovation of Seed Design, Chinese Academy of Sciences, Wuhan 430072, P.R. China.
  • 4 State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, P.R. China; The Key Laboratory of Aquaculture Disease Control, Ministry of Agriculture, Wuhan 430072, P.R. China; University of Chinese Academy of Sciences, Beijing 100049, P.R. China; The Innovation of Seed Design, Chinese Academy of Sciences, Wuhan 430072, P.R. China; Hubei Hongshan Laboratory, Wuhan 430070, P.R. China. Electronic address: [email protected].
PMID: 34171297 DOI: 10.1016/j.molcel.2021.06.004
Abstract

Accurate control of innate immune responses is required to eliminate invading pathogens and simultaneously avoid autoinflammation and autoimmune diseases. Here, we demonstrate that arginine monomethylation precisely regulates the mitochondrial antiviral-signaling protein (MAVS)-mediated Antiviral response. Protein arginine methyltransferase 7 (PRMT7) forms aggregates to catalyze MAVS monomethylation at arginine residue 52 (R52), attenuating its binding to TRIM31 and RIG-I, which leads to the suppression of MAVS aggregation and subsequent activation. Upon virus Infection, aggregated PRMT7 is disabled in a timely manner due to automethylation at arginine residue 32 (R32), and SMURF1 is recruited to PRMT7 by MAVS to induce proteasomal degradation of PRMT7, resulting in the relief of PRMT7 suppression of MAVS activation. Therefore, we not only reveal that arginine monomethylation by PRMT7 negatively regulates MAVS-mediated Antiviral signaling in vitro and in vivo but also uncover a mechanism by which PRMT7 is tightly controlled to ensure the timely activation of Antiviral defense.

Keywords

MAVS; PRMT7; RIG-I; SMUFR1; TRIM31; arginine monomethylation; automethylation; innate immunity; virus infection.

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