Journal
MOLECULAR IMMUNOLOGY
Volume 109, Issue -, Pages 116-125Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2019.02.019
Keywords
IRF7; TRAF6; TARBP2; Ubiquitination; Phosphorylation
Categories
Funding
- National Natural Science Foundation of China [31370876, 31570876]
- Natural Science Foundation of Jiangxi Province [20143ACB20004, 20161BAB204177]
- Open Project Program of Key Laboratory of Functional Small Organic Molecule
- Jiangxi Normal University [KLFS-KF-201407]
- Ministry of Education
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Interferon regulatory factor 7 (IRF7), a crucial regulator of type I interferons (IFNs), plays a crucial role in resistance to viral infection. The abnormal production of type I IFNs is associated with many types of disease, such as cancer and inflammatory disorders. Thus, understanding the post-translational modifications of IRF7 is essential to promoting an appropriate immune response. We have recently showed that the TAR RNA binding protein 2 (TARBP2) suppresses IFN-beta production and the innate antiviral response by targeting MAVS. Here, we further identified TARBP2 as a novel inhibitor of IRF7, which inhibits IRF7-mediated IFN-beta production triggered by the Sendai virus in 293 T cells. Overexpression of TARBP2 inhibits the phosphorylation as well as the K63-linked ubiquitination of IRF7, whilst TARBP2 also impairs the stability of endogenous TRAF6. Furthermore, TARBP2 participates in the interaction between IRF7 and TRAF6, thereby suppressing TRAF6-mediated K63-linked ubiquitination of IRF7, which is a prerequisite of IRF7 phosphorylation. Our findings further reveal the mechanism by which TARBP2 regulates the antiviral signaling pathways of the innate immune system.
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