UFL1 promotes antiviral immune response by maintaining STING stability independent of UFMylation |
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| Authors: | Yijie Tao Shulei Yin Yang Liu Chunzhen Li Yining Chen Dan Han Jingyi Huang Sheng Xu Zui Zou Yizhi Yu |
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| Affiliation: | 1.National Key Laboratory of Medical Immunology and Institute of Immunology, Naval Medical University, Shanghai, 200433 China ;2.Department of Anesthesiology, Changzheng Hospital, Second Affiliated Hospital of Naval Medical University, Shanghai, 200003 China ;3.School of Anesthesiology, Naval Medical University, 168 Changhai Road, Shanghai, 200433 China |
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| Abstract: | The precise regulation of STING homeostasis is essential for its antiviral function. Post-translational modification, especially ubiquitination, is important for the regulation of STING homeostasis. Previous studies have focused on how STING is degraded, but little is known about its maintenance. Here, we show that UFM1 specific ligase UFL1 promotes innate immune response by maintaining STING expression independent of UFMylation. Mechanistically, UFL1 inhibits TRIM29 to interact with STING, thereby reducing its ubiquitination at K338/K347/K370 and subsequent proteasomal degradation. DNA virus infection reduces the UFL1 expression, which may promote STING degradation and facilitate viral expansion. Our study identifies UFL1 as a crucial regulator for the maintenance of STING stability and antiviral function, and provides novel insights into the mechanistic explanation for the immunological escape of DNA virus.Subject terms: Cell death and immune response, Ubiquitylation |
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