ArticleThe Biochemical journal2017
Identification of TBK1 complexes required for the phosphorylation of IRF3 and the production of interferon β.
Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 62 citations in OpenAlex.
- Interferon Regulatory Factors as Potential Therapeutic Targets in Cardiovascular Disease: Focusing on Vascular Inflammation.International journal of molecular sciences · 2026Review
- "CANDLE syndrome: A closer look at a rare autoinflammatory disorder".Journal of translational autoimmunity · 2026Review
- The potential of H5N1 viruses to adapt to bovine cells varies throughout evolution.Nature communications · 2025Article
- African swine fever virus L11L interferes with antiviral responses by targeting the IRF3 and PKR.Cellular and molecular life sciences : CMLS · 2025Article
- Analysis of the Virus-Host Protein-Protein Interaction via Co-Immunoprecipitation (Co-IP).Methods in molecular biology (Clifton, N.J.) · 2025Article
- Cytokine-like-Vago-mediated antiviral response iniScience · 2024Article
- Seneca Valley virus 3C protease cleaves OPTN (optineurin) to Impair selective autophagy and type I interferon signaling.Autophagy · 2024Article
- Kinome-wide siRNA screen identifies a DCLK2-TBK1 oncogenic signaling axis in clear cell renal cell carcinoma.Molecular cell · 2024Article
- NAK-associated protein 1/NAP1 activates TBK1 to ensure accurate mitosis and cytokinesis.The Journal of cell biology · 2024Article
- Article
- A bacterial autotransporter impairs innate immune responses by targeting the transcription factor TFE3.Nature communications · 2023Article
- Rintatolimod: a potential treatment in patients with pancreatic cancer expressing Toll-like receptor 3.American journal of cancer research · 2023Article
- TBK1 is part of a galectin 8 dependent membrane damage recognition complex and drives autophagy upon Adenovirus endosomal escape.PLoS pathogens · 2022Article
- Optineurin in ocular herpes infection.Experimental eye research · 2022Review
- The role of TBK1 in cancer pathogenesis and anticancer immunity.Journal of experimental & clinical cancer research : CR · 2022Review
- MAGI1 inhibits interferon signaling to promote influenza A infection.Frontiers in cardiovascular medicine · 2022Article
- OPTN is a host intrinsic restriction factor against neuroinvasive HSV-1 infection.Nature communications · 2021Article
- TBK1 Inhibitor Exerts Antiproliferative Effect on Glioblastoma Multiforme Cells.Oncology research · 2021Article
- Article
- Circular RNA circDtx1 regulates IRF3-mediated antiviral immune responses through suppression of miR-15a-5p-dependent TRIF downregulation in teleost fish.PLoS pathogens · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The double-stranded RNA mimetic poly(I:C) and lipopolysaccharide (LPS) activate Toll-like receptors 3 (TLR3) and TLR4, respectively, triggering the activation of TANK (TRAF family member-associated NF-κB activator)-binding kinase 1 (TBK1) complexes, the phosphorylation of interferon regulatory factor 3 (IRF3) and transcription of the interferon β (IFNβ) gene. Here, we demonstrate that the TANK-TBK1 and optineurin (OPTN)-TBK1 complexes control this pathway. The poly(I:C)- or LPS-stimulated phosphorylation of IRF3 at Ser396 and production of IFNβ were greatly reduced in bone marrow-derived macrophages (BMDMs) from TANK knockout (KO) mice crossed to knockin mice expressing the ubiquitin-binding-defective OPTN[D477N] mutant. In contrast, IRF3 phosphorylation and IFNβ production were not reduced significantly in BMDM from OPTN[D477N] knockin mice and only reduced partially in TANK KO BMDM. The TLR3/TLR4-dependent phosphorylation of IRF3 and IFNβ gene transcription were not decreased in macrophages from OPTN[D477N] crossed to mice deficient in IκB kinase ε, a TANK-binding kinase related to TBK1. In contrast with the OPTN-TBK1 complex, TBK1 associated with OPTN[D477N] did not undergo phosphorylation at Ser172 in response to poly(I:C) or LPS, indicating that the interaction of ubiquitin chains with OPTN is required to activate OPTN-TBK1 in BMDM. The phosphorylation of IRF3 and IFNβ production induced by Sendai virus infection were unimpaired in BMDM from TANK KO × OPTN[D477N] mice, suggesting that other/additional TBK1 complexes control the RIG-I-like receptor-dependent production of IFNβ. Finally, we present evidence that, in human HACAT cells, the poly(I:C)-dependent phosphorylation of TBK1 at Ser172 involves a novel TBK1-activating kinase(s).
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.