The protein arginine methyltransferase PRMT1 promotes TBK1 activation through asymmetric arginine methylation

Cell Reports

Guimin Zhao¹  Honghai Zhang¹  Hansen Liu¹  Haifeng Wu¹  Feng Liu¹  Yi Zheng¹  Bingyu Liu¹  Lei Zhang¹  Chengjiang Gao¹  Zhenzhen Yan¹  Wanxin Zhuang¹ 

[1] Key Laboratory of Infection and Immunity of Shandong Province and Department of Immunology, School of Biomedical Sciences, Shandong University, Jinan, Shandong 250012, P.R. China;

关键词: protein arginine methylation;    innate antiviral immunity;    PRMT1;    TBK1;   

DOI  :  

来源: DOAJ

【 摘 要 】

Summary: TBK1 is an essential kinase for the innate immune response against viral infection. However, the key molecular mechanisms regulating the TBK1 activation remain elusive. Here, we identify PRMT1, a type I protein arginine methyltransferase, as an essential regulator of TBK1 activation. PRMT1 directly interacts with TBK1 and catalyzes asymmetric methylation of R54, R134, and R228 on TBK1. This modification enhances TBK1 oligomerization after viral infection, which subsequently promotes TBK1 phosphorylation and downstream type I interferon production. More important, myeloid-specific Prmt1 knockout mice are more susceptible to infection with DNA and RNA viruses than Prmt1fl/fl mice. Our findings reveal insights into the molecular regulation of TBK1 activation and demonstrate the essential function of protein arginine methylation in innate antiviral immunity.

【 授权许可】

Unknown