甲基化
先天免疫系统
精氨酸
信号转导衔接蛋白
甲基转移酶
细胞生物学
免疫系统
线粒体
生物
经典补体途径
化学
信号转导
氨基酸
补体系统
生物化学
免疫学
基因
作者
Xuemei Bai,Chao Sui,Feng Liu,Tian Chen,Lei Zhang,Yi Zheng,Bingyu Liu,Chengjiang Gao
标识
DOI:10.1038/s41467-022-32628-y
摘要
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.
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