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Mst1 shuts off cytosolic antiviral defense through IRF3 phosphorylation

Journal article published in 2016 by Fansen Meng, Ruyuan Zhou, Shiying Wu, Qian Zhang, Qiuheng Jin, Yao Zhou, Steven W. Plouffe, Shengduo Liu, Hai Song, Zongping Xia, Bin Zhao, Sheng Ye, Xin-Hua Feng, Kun-Liang Guan, Jian Zou and other authors.
This paper is available in a repository.
This paper is available in a repository.

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Abstract

Here, Meng et al. investigated how interferon regulatory factor 3 (IRF3) activation, a key signal mediator/transcriptional factor of the antiviral-sensing pathway, is regulated. They demonstrate that Mst1, a stress response kinase, represses cytosolic antiviral sensing and defense through the repression of RNA virus-induced activation of TBK1 and interference with the IRF3 homodimerization and chromatin binding via direct phosphorylation of IRF3 Thr253 and Thr75 residues.