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Journal articles on the topic 'TANK-binding kinase 1'

Author: Grafiati

Published: 5 June 2025

Last updated: 1 August 2025

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1

Revach, Or-Yam, Shuming Liu, and Russell W. Jenkins. "Targeting TANK-binding kinase 1 (TBK1) in cancer." Expert Opinion on Therapeutic Targets 24, no. 11 (2020): 1065–78. http://dx.doi.org/10.1080/14728222.2020.1826929.

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2

Durand, Joel, Qing Zhang та Albert Baldwin. "Roles for the IKK-Related Kinases TBK1 and IKKε in Cancer". Cells 7, № 9 (2018): 139. http://dx.doi.org/10.3390/cells7090139.

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While primarily studied for their roles in innate immune response, the IκB kinase (IKK)-related kinases TANK-binding kinase 1 (TBK1) and IKKε also promote the oncogenic phenotype in a variety of cancers. Additionally, several substrates of these kinases control proliferation, autophagy, cell survival, and cancer immune responses. Here we review the involvement of TBK1 and IKKε in controlling different cancers and in regulating responses to cancer immunotherapy.

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3

Tu, Daqi, Zehua Zhu, Alicia Y. Zhou, et al. "Structure and Ubiquitination-Dependent Activation of TANK-Binding Kinase 1." Cell Reports 3, no. 3 (2013): 747–58. http://dx.doi.org/10.1016/j.celrep.2013.01.033.

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4

Ma, X., E. Helgason, Q. T. Phung, et al. "Molecular basis of Tank-binding kinase 1 activation by transautophosphorylation." Proceedings of the National Academy of Sciences 109, no. 24 (2012): 9378–83. http://dx.doi.org/10.1073/pnas.1121552109.

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5

Xie, X., D. Zhang, B. Zhao, et al. "I B kinase and TANK-binding kinase 1 activate AKT by direct phosphorylation." Proceedings of the National Academy of Sciences 108, no. 16 (2011): 6474–79. http://dx.doi.org/10.1073/pnas.1016132108.

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6

Sawal, Humaira Aziz, Shagufta Nighat, Tanzeela Safdar, and Laiba Anees. "Comparative In Silico Analysis and Functional Characterization of TANK-Binding Kinase 1–Binding Protein 1." Bioinformatics and Biology Insights 17 (January 2023): 117793222311648. http://dx.doi.org/10.1177/11779322231164828.

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Protein modelling plays a vital role in the drug discovery process. TANK-binding kinase 1–binding protein 1 is also called an adapter protein, which is encoded by gene TBK1 present in Homo sapiens. It is found in lungs, small intestine, leukocytes, heart, placenta, muscle, kidney, lower level of thymus, and brain. It has a number of protein-binding sites, to which TBK1 and IKBKE bind and perform different functions as immunomodulatory, antiproliferative, and antiviral innate immunity which release different types of interferons. Our study predicts the comparative model of 3-dimensional (3D) st

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7

Zhang, Wanqiao, Jian Wang, Ying Zhang та ін. "The Scaffold Protein TANK/I-TRAF Inhibits NF-κB Activation by Recruiting Polo-like Kinase 1". Molecular Biology of the Cell 21, № 14 (2010): 2500–2513. http://dx.doi.org/10.1091/mbc.e09-08-0715.

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TANK/I-TRAF is a TRAF-binding protein that negatively regulates NF-κB activation. The underlying mechanism of this activity remains unclear. Here we show that TANK directly interacts with PLK1, a conserved cell cycle–regulated kinase. PLK1 inhibits NF-κB transcriptional activation induced by TNF-α, IL-1β, or several activators, but not by nuclear transcription factor p65. PLK1 expression reduces the DNA-binding activity of NF-κB induced by TNF-α. Moreover, endogenous activation of PLK1 reduces the TNF-induced phosphorylation of endogenous IκBα. PLK1 is bound to NEMO (IKKγ) through TANK to form

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8

Larabi, Amede, Juliette M. Devos, Sze-Ling Ng, et al. "Crystal Structure and Mechanism of Activation of TANK-Binding Kinase 1." Cell Reports 3, no. 3 (2013): 734–46. http://dx.doi.org/10.1016/j.celrep.2013.01.034.

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9

Bakshi, Siddharth, Jordan Taylor, Sam Strickson, Thomas McCartney та Philip Cohen. "Identification of TBK1 complexes required for the phosphorylation of IRF3 and the production of interferon β". Biochemical Journal 474, № 7 (2017): 1163–74. http://dx.doi.org/10.1042/bcj20160992.

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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 macro

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10

Zhao, Chunyuan, and Wei Zhao. "TANK-binding kinase 1 as a novel therapeutic target for viral diseases." Expert Opinion on Therapeutic Targets 23, no. 5 (2019): 437–46. http://dx.doi.org/10.1080/14728222.2019.1601702.

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11

Cruz, Victoria H., and Rolf A. Brekken. "Assessment of TANK-binding kinase 1 as a therapeutic target in cancer." Journal of Cell Communication and Signaling 12, no. 1 (2017): 83–90. http://dx.doi.org/10.1007/s12079-017-0438-y.

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12

Ye, Junqiang, Jonah Cheung, Valeria Gerbino, et al. "Effects of ALS-associated TANK binding kinase 1 mutations on protein–protein interactions and kinase activity." Proceedings of the National Academy of Sciences 116, no. 49 (2019): 24517–26. http://dx.doi.org/10.1073/pnas.1915732116.

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Exonic DNA sequence variants in the Tbk1 gene associate with both sporadic and familial amyotrophic lateral sclerosis (ALS). Here, we examine functional defects in 25 missense TBK1 mutations, focusing on kinase activity and protein–protein interactions. We identified kinase domain (KD) mutations that abolish kinase activity or display substrate-specific defects in specific pathways, such as innate immunity and autophagy. By contrast, mutations in the scaffold dimerization domain (SDD) of TBK1 can cause the loss of kinase activity due to structural disruption, despite an intact KD. Familial ALS

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13

Ma, Y., H. Jin, T. Valyi-Nagy, Y. Cao, Z. Yan, and B. He. "Inhibition of TANK Binding Kinase 1 by Herpes Simplex Virus 1 Facilitates Productive Infection." Journal of Virology 86, no. 4 (2011): 2188–96. http://dx.doi.org/10.1128/jvi.05376-11.

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14

Huang, Li, Tao Xiong, Huibin Yu та ін. "Encephalomyocarditis virus 3C protease attenuates type I interferon production through disrupting the TANK–TBK1–IKKε–IRF3 complex". Biochemical Journal 474, № 12 (2017): 2051–65. http://dx.doi.org/10.1042/bcj20161037.

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TRAF family member-associated NF-κB activator (TANK) is a scaffold protein that assembles into the interferon (IFN) regulator factor 3 (IRF3)-phosphorylating TANK-binding kinase 1 (TBK1)–(IκB) kinase ε (IKKε) complex, where it is involved in regulating phosphorylation of the IRF3 and IFN production. However, the functions of TANK in encephalomyocarditis virus (EMCV) infection-induced type I IFN production are not fully understood. Here, we demonstrated that, instead of stimulating type I IFN production, the EMCV-HB10 strain infection potently inhibited Sendai virus- and polyI:C-induced IRF3 ph

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15

Li, Shun, Long-Feng Lu, Scott E. LaPatra, Dan-Dan Chen та Yong-An Zhang. "Zebrafish STAT6 negatively regulates IFNφ1 production by attenuating the kinase activity of TANK-binding kinase 1". Developmental & Comparative Immunology 67 (лютий 2017): 189–201. http://dx.doi.org/10.1016/j.dci.2016.10.003.

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16

Hui, Lu, Xiaolin Chen, Mengke Huang, Yongmei Jiang, and Ting Liu. "TANK-Binding Kinase 1 in the Pathogenesis and Treatment of Inflammation-Related Diseases." International Journal of Molecular Sciences 26, no. 5 (2025): 1941. https://doi.org/10.3390/ijms26051941.

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TANK-binding kinase 1 (TBK1) is a key signaling kinase involved in innate immune and inflammatory responses. TBK1 drives immune cells to participate in the inflammatory response by activating the NF-κB and interferon regulatory factor signaling pathways in immune cells, promoting the expression of pro-inflammatory genes, and regulating immune cell function. Thus, it plays a crucial role in initiating a signaling cascade that establishes an inflammatory environment. In inflammation-related diseases, TBK1 acts as a bridge linking inflammation to immunity, metabolism, or tumorigenesis, playing an

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17

Herhaus, Lina. "TBK1 (TANK-binding kinase 1)-mediated regulation of autophagy in health and disease." Matrix Biology 100-101 (June 2021): 84–98. http://dx.doi.org/10.1016/j.matbio.2021.01.004.

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18

Alam, Manzar, Gulam Mustafa Hasan, and Md Imtaiyaz Hassan. "A review on the role of TANK-binding kinase 1 signaling in cancer." International Journal of Biological Macromolecules 183 (July 2021): 2364–75. http://dx.doi.org/10.1016/j.ijbiomac.2021.06.022.

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19

Ishii, Ken J., Tatsukata Kawagoe, Shohei Koyama, et al. "TANK-binding kinase-1 delineates innate and adaptive immune responses to DNA vaccines." Nature 451, no. 7179 (2008): 725–29. http://dx.doi.org/10.1038/nature06537.

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20

Wei, Congwen, Yuan Cao, Xiaoli Yang, et al. "Elevated expression of TANK-binding kinase 1 enhances tamoxifen resistance in breast cancer." Proceedings of the National Academy of Sciences 111, no. 5 (2014): E601—E610. http://dx.doi.org/10.1073/pnas.1316255111.

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21

Husain, Shahrukh, Vijay Kumar, and Md Imtaiyaz Hassan. "Phosphorylation-induced changes in the energetic frustration in human Tank binding kinase 1." Journal of Theoretical Biology 449 (July 2018): 14–22. http://dx.doi.org/10.1016/j.jtbi.2018.04.016.

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22

Tang, Xueying, Baoyu Huang, Linlin Zhang, Li Li, and Guofan Zhang. "TANK-binding kinase-1 broadly affects oyster immune response to bacteria and viruses." Fish & Shellfish Immunology 56 (September 2016): 330–35. http://dx.doi.org/10.1016/j.fsi.2016.07.011.

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23

Lv, Ping, Congye Li, Meihui Wang, Jun Ren, Yingmei Zhang, and Guosheng Fu. "TANK-binding kinase 1 alleviates myocardial ischemia/reperfusion injury through regulating apoptotic pathway." Biochemical and Biophysical Research Communications 528, no. 3 (2020): 574–79. http://dx.doi.org/10.1016/j.bbrc.2020.05.143.

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24

Lv, Huifang, Wang Dong, Zhi Cao, et al. "Classical swine fever virus non-structural protein 4B binds tank-binding kinase 1." Journal of Biosciences 43, no. 5 (2018): 947–57. http://dx.doi.org/10.1007/s12038-018-9802-1.

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25

Cho, Chun‐Seok, Hwan‐Woo Park, Allison Ho, et al. "Lipotoxicity induces hepatic protein inclusions through TANK binding kinase 1–mediated p62/sequestosome 1 phosphorylation." Hepatology 68, no. 4 (2018): 1331–46. http://dx.doi.org/10.1002/hep.29742.

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26

Gleason, Catherine E., Alban Ordureau, Robert Gourlay, J. Simon C. Arthur та Philip Cohen. "Polyubiquitin Binding to Optineurin Is Required for Optimal Activation of TANK-binding Kinase 1 and Production of Interferon β". Journal of Biological Chemistry 286, № 41 (2011): 35663–74. http://dx.doi.org/10.1074/jbc.m111.267567.

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TANK-binding kinase (TBK1) is essential for transcription of the interferon (IFN) β gene in response to lipopolysaccharide (LPS) and double-stranded RNA, but the molecular mechanisms that underlie the activation of TBK1 are incompletely understood. Previously, we identified the NF-κB essential modulator (NEMO)-related polyubiquitin-binding protein, optineurin (OPTN), as a novel binding partner of TBK1. To determine whether the ubiquitin-binding function of OPTN is involved in regulating TBK1 and IFNβ production, we generated a mouse in which wild-type optineurin was replaced by the polyubiquit

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27

Wang, Lijuan, Lei Zhang, Xueying Zhao, Meng Zhang, Wei Zhao та Chengjiang Gao. "Lithium Attenuates IFN-β Production and Antiviral Response via Inhibition of TANK-Binding Kinase 1 Kinase Activity". Journal of Immunology 191, № 8 (2013): 4392–98. http://dx.doi.org/10.4049/jimmunol.1203142.

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28

Huh, Jin Young, та Alan R. Saltiel. "Roles of IκB kinases and TANK-binding kinase 1 in hepatic lipid metabolism and nonalcoholic fatty liver disease". Experimental & Molecular Medicine 53, № 11 (2021): 1697–705. http://dx.doi.org/10.1038/s12276-021-00712-w.

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AbstractNonalcoholic fatty liver disease (NAFLD) is the most common cause of chronic liver disease and is strongly associated with obesity-related ectopic fat accumulation in the liver. Hepatic lipid accumulation encompasses a histological spectrum ranging from simple steatosis to nonalcoholic steatohepatitis (NASH), which can progress to cirrhosis and hepatocellular carcinoma. Given that dysregulated hepatic lipid metabolism may be an onset factor in NAFLD, understanding how hepatic lipid metabolism is modulated in healthy subjects and which steps are dysregulated in NAFLD subjects is crucial

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29

Clark, Kristopher, Mark Peggie, Lorna Plater, et al. "Novel cross-talk within the IKK family controls innate immunity." Biochemical Journal 434, no. 1 (2011): 93–104. http://dx.doi.org/10.1042/bj20101701.

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Members of the IKK {IκB [inhibitor of NF-κB (nuclear factor κB)] kinase} family play a central role in innate immunity by inducing NF-κB- and IRF [IFN (interferon) regulatory factor]-dependent gene transcription programmes required for the production of pro-inflammatory cytokines and IFNs. However, the molecular mechanisms that activate these protein kinases and their complement of physiological substrates remain poorly defined. Using MRT67307, a novel inhibitor of IKKϵ/TBK1 (TANK {TRAF [TNF (tumour-necrosis-factor)-receptor-associated factor]-associated NF-κB activator}-binding kinase 1) and

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30

Goh, Eddy T. H., J. Simon C. Arthur, Peter C. F. Cheung, Shizuo Akira, Rachel Toth, and Philip Cohen. "Identification of the protein kinases that activate the E3 ubiquitin ligase Pellino 1 in the innate immune system." Biochemical Journal 441, no. 1 (2011): 339–46. http://dx.doi.org/10.1042/bj20111415.

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The E3 ubiquitin ligase Pellino 1 can be interconverted between inactive and active forms by a reversible phosphorylation mechanism. In vitro, phosphorylation and activation can be catalysed by either the IRAKs [IL (interleukin)-1-receptor-associated kinases] IRAK1 and IRAK4, or the IKK {IκB [inhibitor of NF-κB (nuclear factor κB)] kinase}-related kinases [IKKϵ and TBK1 (TANK {TRAF [TNF (tumour-necrosis-factor)-receptor-associated factor]-associated NF-κB activator}-binding kinase 1)]. In the present study we establish that IRAK1 is the major protein kinase that mediates the IL-1-stimulated ac

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31

Ahmad, Liyana, Bayarchimeg Mashbat, Corwin Leung, et al. "Human TANK-binding kinase 1 is required for early autophagy induction upon herpes simplex virus 1 infection." Journal of Allergy and Clinical Immunology 143, no. 2 (2019): 765–69. http://dx.doi.org/10.1016/j.jaci.2018.09.013.

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32

Verpooten, Dustin, Yijie Ma, Songwang Hou, Zhipeng Yan та Bin He. "Control of TANK-binding Kinase 1-mediated Signaling by the γ134.5 Protein of Herpes Simplex Virus 1". Journal of Biological Chemistry 284, № 2 (2008): 1097–105. http://dx.doi.org/10.1074/jbc.m805905200.

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33

Wang, Yaping, Zhongyuan Lu, Zhangwei Hu, et al. "The up-regulation of TANK-binding kinase 1 in head and neck squamous cell carcinoma." Translational Cancer Research 6, no. 4 (2017): 679–86. http://dx.doi.org/10.21037/tcr.2017.08.01.

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34

Zhang, Yanyu, Ragaseema Valsala Madhavan Unnithan, Anahita Hamidi, et al. "TANK‐binding kinase 1 is a mediator of platelet‐induced EMT in mammary carcinoma cells." FASEB Journal 33, no. 7 (2019): 7822–32. http://dx.doi.org/10.1096/fj.201801936rrr.

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35

Delhase, M., S. Y. Kim, H. Lee, et al. "TANK-binding kinase 1 (TBK1) controls cell survival through PAI-2/serpinB2 and transglutaminase 2." Proceedings of the National Academy of Sciences 109, no. 4 (2011): E177—E186. http://dx.doi.org/10.1073/pnas.1119296109.

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36

Marineau, Alexandre, Kashif Aziz Khan та Marc J. Servant. "Roles of GSK-3 and β-Catenin in Antiviral Innate Immune Sensing of Nucleic Acids". Cells 9, № 4 (2020): 897. http://dx.doi.org/10.3390/cells9040897.

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The rapid activation of the type I interferon (IFN) antiviral innate immune response relies on ubiquitously expressed RNA and DNA sensors. Once engaged, these nucleotide-sensing receptors use distinct signaling modules for the rapid and robust activation of mitogen-activated protein kinases (MAPKs), the IκB kinase (IKK) complex, and the IKK-related kinases IKKε and TANK-binding kinase 1 (TBK1), leading to the subsequent activation of the activator protein 1 (AP1), nuclear factor-kappa B (NF-κB), and IFN regulatory factor 3 (IRF3) transcription factors, respectively. They, in turn, induce immun

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37

Muñoz, Marina C., Jorge F. Giani, Marcos A. Mayer, Jorge E. Toblli, Daniel Turyn, and Fernando P. Dominici. "TANK-binding kinase 1 mediates phosphorylation of insulin receptor at serine residue 994: a potential link between inflammation and insulin resistance." Journal of Endocrinology 201, no. 2 (2009): 185–97. http://dx.doi.org/10.1677/joe-08-0276.

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The IκB kinase-β (IKK-β)/nuclear factor-κB signaling pathway has been suggested to link inflammation with obesity and insulin resistance. In addition, angiotensin (Ang) II is able to induce insulin resistance and an inflammatory state through Ang II receptor type 1 (AT1R). Accordingly, we examined whether inhibition of AT1R with irbesartan (IRB) can protect against the development of insulin resistance in obese Zucker rats (OZRs). IRB-treatment improved the insulin-stimulated insulin receptor (IR) phosphorylation at tyrosine (Tyr) residues 1158, 1162, 1163 (involved in activation of the IR kin

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38

Prins, Kathleen C., Washington B. Cárdenas та Christopher F. Basler. "Ebola Virus Protein VP35 Impairs the Function of Interferon Regulatory Factor-Activating Kinases IKKε and TBK-1". Journal of Virology 83, № 7 (2009): 3069–77. http://dx.doi.org/10.1128/jvi.01875-08.

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ABSTRACT The Ebola virus (EBOV) VP35 protein antagonizes the early antiviral alpha/beta interferon (IFN-α/β) response. We previously demonstrated that VP35 inhibits the virus-induced activation of the IFN-β promoter by blocking the phosphorylation of IFN-regulatory factor 3 (IRF-3), a transcription factor that is crucial for the induction of IFN-α/β expression. Furthermore, VP35 blocks IFN-β promoter activation induced by any of several components of the retinoic acid-inducible gene I (RIG-I)/melanoma differentiation-associated gene 5 (MDA-5)-activated signaling pathways including RIG-I, IFN-β

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39

Bibeau-Poirier, A., S. P. Gravel, J. F. Clément та ін. "Involvement of the IκB kinase (IKK)-related kinases tank-binding kinase 1/IKKi and cullin-based ubiquitin ligases in IFN regulatory factor-3 degradation". Journal of Immunology 177, № 12 (2006): 8878.3–8879. http://dx.doi.org/10.4049/jimmunol.177.12.8878-b.

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40

Bibeau-Poirier, Annie, Simon-Pierre Gravel, Jean-François Clément та ін. "Involvement of the IκB Kinase (IKK)-Related Kinases Tank-Binding Kinase 1/IKKi and Cullin-Based Ubiquitin Ligases in IFN Regulatory Factor-3 Degradation". Journal of Immunology 177, № 8 (2006): 5059–67. http://dx.doi.org/10.4049/jimmunol.177.8.5059.

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41

Bist, Pradeep, Shinla Shu, Huiyin Lee та ін. "Annexin-A1 Regulates TLR-Mediated IFN-β Production through an Interaction with TANK-Binding Kinase 1". Journal of Immunology 191, № 8 (2013): 4375–82. http://dx.doi.org/10.4049/jimmunol.1301504.

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42

Li, Manru, Yu Zhou, Tiantian Wang, et al. "Nintedanib exerts anti-pulmonary fibrosis activity via inhibiting TANK-binding kinase 1 (TBK1) phosphorylation." Chemical Communications 58, no. 8 (2022): 1199–202. http://dx.doi.org/10.1039/d1cc05621b.

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We described a chemoproteomics approach to identify TBK1 as a key target of the multikinase inhibitor nintedanib in IPF. This insight may facilitate a better understanding of the functional mechanism of nintedanib for antifibrosis efficacy.

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43

Hammaker, D., D. L. Boyle, and G. S. Firestein. "Synoviocyte innate immune responses: TANK-binding kinase-1 as a potential therapeutic target in rheumatoid arthritis." Rheumatology 51, no. 4 (2011): 610–18. http://dx.doi.org/10.1093/rheumatology/ker154.

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44

Delint-Ramirez, Ilse, Roger Maldonado Ruiz, Ivan Torre-Villalvazo, et al. "Genetic obesity alters recruitment of TANK-binding kinase 1 and AKT into hypothalamic lipid rafts domains." Neurochemistry International 80 (January 2015): 23–32. http://dx.doi.org/10.1016/j.neuint.2014.11.002.

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45

Wang, Lingyan, Shitao Li, and Martin E. Dorf. "NEMO Binds Ubiquitinated TANK-Binding Kinase 1 (TBK1) to Regulate Innate Immune Responses to RNA Viruses." PLoS ONE 7, no. 9 (2012): e43756. http://dx.doi.org/10.1371/journal.pone.0043756.

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46

Louis, Cynthia, Devi Ngo, Damian B. D'Silva, et al. "Therapeutic Effects of a TANK ‐Binding Kinase 1 Inhibitor in Germinal Center–Driven Collagen‐Induced Arthritis." Arthritis & Rheumatology 71, no. 1 (2018): 50–62. http://dx.doi.org/10.1002/art.40670.

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47

Fu, Tao, Mingfang Zhang, Zixuan Zhou, et al. "Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52." Science Advances 7, no. 33 (2021): eabi6582. http://dx.doi.org/10.1126/sciadv.abi6582.

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The recruitment of Unc-51-like kinase and TANK-binding kinase 1 complexes is essential for Nuclear dot protein 52-mediated selective autophagy and relies on the specific association of NDP52, RB1-inducible coiled-coil protein 1, and Nak-associated protein 1 (5-azacytidine-induced protein 2, AZI2). However, the underlying molecular mechanism remains elusive. Here, we find that except for the NDP52 SKIP carboxyl homology (SKICH)/RB1CC1 coiled-coil interaction, the LC3-interacting region of NDP52 can directly interact with the RB1CC1 Claw domain, as that of NAP1 FIP200-binding region (FIR). The d

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48

Hikichi, Miyako, Hirotaka Toh, Atsuko Minowa-Nozawa, Takashi Nozawa, and Ichiro Nakagawa. "Guanylate-Binding Protein 1 Regulates Infection-Induced Autophagy through TBK1 Phosphorylation." Cellular Microbiology 2022 (May 29, 2022): 1–18. http://dx.doi.org/10.1155/2022/8612113.

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Invading bacteria can be degraded by selective autophagy, known as xenophagy. Recent studies have shown that the recruitment of autophagy adaptor proteins such as p62 to bacteria and its regulation by activated TANK-binding kinase 1 (TBK1) are required to overcome bacterial infection. However, the detailed molecular mechanisms behind this are not yet fully understood. Here, we show that the human guanylate-binding protein (GBP) family, especially GBP1, directs xenophagy against invading Group A Streptococcus (GAS) by promoting TBK1 phosphorylation. GBP1 exhibits a GAS-surrounding localization

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49

Verpooten, Dustin, Zongdi Feng, Tibor Valyi-Nagy та ін. "Dephosphorylation of eIF2α Mediated by the γ134.5 Protein of Herpes Simplex Virus 1 Facilitates Viral Neuroinvasion". Journal of Virology 83, № 23 (2009): 12626–30. http://dx.doi.org/10.1128/jvi.01431-09.

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ABSTRACT The γ134.5 protein, a virulence factor of herpes simplex viruses, redirects protein phosphatase 1 to dephosphorylate the α subunit of translation initiation factor 2 (eIF2α). Additionally, it inhibits the induction of antiviral genes by TANK-binding kinase 1. Nevertheless, its precise role in vivo remains to be established. Here we show that eIF2α dephosphorylation by γ134.5 is crucial for viral neuroinvasion. V193E and F195L substitutions in γ134.5 abrogate viral replication in the eye and spread to the trigeminal ganglia and brain. Intriguingly, inhibition of antiviral gene inductio

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50

Möller, Moritz, Julia Wasel, Julia Schmetzer та ін. "The Specific IKKε/TBK1 Inhibitor Amlexanox Suppresses Human Melanoma by the Inhibition of Autophagy, NF-κB and MAP Kinase Pathways". International Journal of Molecular Sciences 21, № 13 (2020): 4721. http://dx.doi.org/10.3390/ijms21134721.

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Abstract:

Inhibitor-kappaB kinase epsilon (IKKε) and TANK-binding kinase 1 (TBK1) are non-canonical IκB kinases, both described as contributors to tumor growth and metastasis in different cancer types. Several hints indicate that they are also involved in the pathogenesis of melanoma; however, the impact of their inhibition as a potential therapeutic measure in this “difficult-to-treat” cancer type has not been investigated so far. We assessed IKKε and TBK1 expression in human malignant melanoma cells, primary tumors and the metastasis of melanoma patients. Both kinases were expressed in the primary tum

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