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Updated: Aug 5, 2025

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
Published on: January 24, 2016
p120-catenin promotes innate antiviral immunity through stabilizing TBK1-IRF3 complex
Haifeng Wu1, Xiuqing Yan1, Liang Zhao1
1Shandong Provincial Qianfoshan Hospital, Shandong University, No. 16766 Jingshi Road, Jinan 250014, Shandong, China; Department of Anesthesiology and Perioperative Medicine, The First Affiliated Hospital of Shandong First Medical University, Shandong Institute of Anesthesia and Respiratory Critical Care Medicine, No. 16766 Jingshi Road, Jinan 250014, Shandong, China.
Abstract:
TBK1-IRF3 complex plays vital roles in antiviral immune responses, its regulatory mechanisms are currently incompletely understood. p120-catenin (p120), an armadillo-repeat protein, mainly regulates the stability of classical cadherins and the development of epithelial-to-mesenchymal transitions (EMTs). Here we report that p120 is a positive regulator of type I IFN production. Ectopic expression of p120 enhanced Vesicular stomatitis virus and Sendai-virus-induced type I IFN production, whereas knockdown of p120 expression suppressed type I IFN production. Mechanistically, p120 promoted phosphorylation of IRF3 via stabilizing the TBK1-IRF3 complex. Consistently, p120 knock down mice are more susceptible to VSV infection as indicated by higher tissue viral titers, less IFN-I production and greater infiltration of immune cells. This study reveals p120 as an important positive regulator in innate immunity and identifies that p120 facilitates host antiviral response through stabilizing TBK1-IRF3 complex.
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