The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation
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 h...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-32628-y |
| _version_ | 1797363179410423808 |
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| author | Xuemei Bai Chao Sui Feng Liu Tian Chen Lei Zhang Yi Zheng Bingyu Liu Chengjiang Gao |
| author_facet | Xuemei Bai Chao Sui Feng Liu Tian Chen Lei Zhang Yi Zheng Bingyu Liu Chengjiang Gao |
| author_sort | Xuemei Bai |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-08T16:17:19Z |
| format | Article |
| id | doaj.art-61b9c81825fb4c8aa89b5bc6a4883f80 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-03-08T16:17:19Z |
| publishDate | 2022-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-61b9c81825fb4c8aa89b5bc6a4883f802024-01-07T12:31:55ZengNature PortfolioNature Communications2041-17232022-08-0113111610.1038/s41467-022-32628-yThe protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylationXuemei Bai0Chao Sui1Feng Liu2Tian Chen3Lei Zhang4Yi Zheng5Bingyu Liu6Chengjiang Gao7Key Laboratory of Infection and Immunity of Shandong Province & Department of Immunology, School of Basic Medical Sciences, Shandong UniversityKey Laboratory of Infection and Immunity of Shandong Province & Department of Immunology, School of Basic Medical Sciences, Shandong UniversityKey Laboratory of Infection and Immunity of Shandong Province & Department of Immunology, School of Basic Medical Sciences, Shandong UniversityDepartment of Pathogenic Biology, School of Biomedical Sciences, Shandong UniversityKey Laboratory of Infection and Immunity of Shandong Province & Department of Immunology, School of Basic Medical Sciences, Shandong UniversityKey Laboratory of Infection and Immunity of Shandong Province & Department of Immunology, School of Basic Medical Sciences, Shandong UniversityKey Laboratory of Infection and Immunity of Shandong Province & Department of Immunology, School of Basic Medical Sciences, Shandong UniversityKey Laboratory of Infection and Immunity of Shandong Province & Department of Immunology, School of Basic Medical Sciences, Shandong UniversityAbstract 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.https://doi.org/10.1038/s41467-022-32628-y |
| spellingShingle | Xuemei Bai Chao Sui Feng Liu Tian Chen Lei Zhang Yi Zheng Bingyu Liu Chengjiang Gao The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation Nature Communications |
| title | The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation |
| title_full | The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation |
| title_fullStr | The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation |
| title_full_unstemmed | The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation |
| title_short | The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation |
| title_sort | protein arginine methyltransferase prmt9 attenuates mavs activation through arginine methylation |
| url | https://doi.org/10.1038/s41467-022-32628-y |
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