2. Academic Validation
  3. TRIM24 facilitates antiviral immunity through mediating K63-linked TRAF3 ubiquitination

TRIM24 facilitates antiviral immunity through mediating K63-linked TRAF3 ubiquitination

  • J Exp Med. 2020 Jul 6;217(7):e20192083. doi: 10.1084/jem.20192083.
Qingchen Zhu 1,  Tao Yu 1,  Shucheng Gan 1,  Yan Wang 1,  Yifei Pei 1,  Qifan Zhao 1,  Siyu Pei 1,  Shumeng Hao 1,  Jia Yuan 1,  Jing Xu 1,  Fajian Hou 2,  Xuefeng Wu 3,  Chao Peng 4,  Ping Wu 4,  Jun Qin 1,  Yichuan Xiao 1
Affiliations

Affiliations

  • 1 Chinese Academy of Sciences Key Laboratory of Tissue Microenvironment and Tumor, Shanghai Institute of Nutrition and Health, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai, China.
  • 2 State Key Laboratory of Molecular Biology, Chinese Academy of Sciences Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, University of Chinese Academy of Sciences, Shanghai, China.
  • 3 Shanghai Institute of Immunology, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
  • 4 National Facility for Protein Science in Shanghai, Zhangjiang Lab, Shanghai, China.
PMID: 32324863 DOI: 10.1084/jem.20192083
Abstract

Ubiquitination is an essential mechanism in the control of Antiviral immunity upon virus Infection. Here, we identify a series of ubiquitination-modulating enzymes that are modulated by vesicular stomatitis virus (VSV). Notably, TRIM24 is down-regulated through direct transcriptional suppression induced by VSV-activated IRF3. Reducing or ablating TRIM24 compromises type I IFN (IFN-I) induction upon RNA virus Infection and thus renders mice more sensitive to VSV Infection. Mechanistically, VSV Infection induces abundant TRIM24 translocation to mitochondria, where TRIM24 binds with TRAF3 and directly mediates K63-linked TRAF3 ubiquitination at K429/K436. This modification of TRAF3 enables its association with MAVS and TBK1, which consequently activates downstream Antiviral signaling. Together, these findings establish TRIM24 as a critical positive regulator in controlling the activation of Antiviral signaling and describe a previously unknown mechanism of TRIM24 function.

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