Abramson, J., Adler, J., Dunger, J., Evans, R., Green, T., Pritzel, A., et al. (2024). Accurate structure prediction of biomolecular interactions with alphafold 3. Nature, 630(8016), 493–500. https://doi.org/10.1038/s41586-024-07487-w
Article PubMed PubMed Central Google Scholar
Adams, J. A. (2003). Activation loop phosphorylation and catalysis in protein kinases: Is there functional evidence for the autoinhibitor model? Biochemistry, 42(3), 601–607. https://doi.org/10.1021/bi020617o
Ahmad, L., Zhang, S. Y., Casanova, J. L., & Sancho-Shimizu, V. (2016). Human TBK1: A gatekeeper of neuroinflammation. Trends in Molecular Medicine, 22(6), 511–527. https://doi.org/10.1016/j.molmed.2016.04.006
Article PubMed PubMed Central Google Scholar
Banavali, N. K., & Roux, B. (2009). Flexibility and charge asymmetry in the activation loop of Src tyrosine kinases. Proteins, 74(2), 378–389. https://doi.org/10.1002/prot.22153
Article PubMed PubMed Central Google Scholar
Chio, A., Logroscino, G., Hardiman, O., Swingler, R., Mitchell, D., Beghi, E., et al. (2009). Prognostic factors in ALS: A critical review. Amyotrophic Lateral Sclerosis : Official Publication of the World Federation of Neurology Research Group on Motor Neuron Diseases, 10(5–6), 310–323. https://doi.org/10.3109/17482960802566824
de Majo, M., Topp, S. D., Smith, B. N., Nishimura, A. L., Chen, H. J., Gkazi, A. S., et al. (2018). ALS-associated missense and nonsense TBK1 mutations can both cause loss of kinase function. Neurobiology of Aging, 71, 266e261–266e210. https://doi.org/10.1016/j.neurobiolaging.2018.06.015
Delhase, M., Hayakawa, M., Chen, Y., & Karin, M. (1999). Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation. Science, 284(5412), 309–313. https://doi.org/10.1126/science.284.5412.309
Fischer, F. A., Demarco, B., Min, F. C. H., Yeap, H. W., De Nardo, D., Chen, K. W., et al. (2025). TBK1 and IKKepsilon prevent premature cell death by limiting the activity of both RIPK1 and NLRP3 death pathways. Science Advances, 11(10), eadq1047. https://doi.org/10.1126/sciadv.adq1047
Article PubMed PubMed Central Google Scholar
Freischmidt, A., Wieland, T., Richter, B., Ruf, W., Schaeffer, V., Muller, K., et al. (2015). Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia. Nature Neuroscience, 18(5), 631–636. https://doi.org/10.1038/nn.4000
Freischmidt, A., Muller, K., Ludolph, A. C., Weishaupt, J. H., & Andersen, P. M. (2017). Association of mutations in TBK1 with sporadic and familial amyotrophic lateral sclerosis and frontotemporal dementia. JAMA Neurology, 74(1), 110–113. https://doi.org/10.1001/jamaneurol.2016.3712
Harding, O., Evans, C. S., Ye, J., Cheung, J., Maniatis, T., & Holzbaur, E. L. F. (2021). ALS- and FTD-associated missense mutations in TBK1 differentially disrupt mitophagy. Proceedings of the National Academy of Sciences of the United States of America. https://doi.org/10.1073/pnas.2025053118
Article PubMed PubMed Central Google Scholar
Hornbeck, P. V., Zhang, B., Murray, B., Kornhauser, J. M., Latham, V., & Skrzypek, E. (2015). PhosphoSitePlus, 2014: Mutations, PTMs and recalibrations. Nucleic Acids Research, 43(Database issue), D512–520. https://doi.org/10.1093/nar/gku1267
Kishore, N., Huynh, Q. K., Mathialagan, S., Hall, T., Rouw, S., Creely, D., et al. (2002). IKK-i and TBK-1 are enzymatically distinct from the homologous enzyme IKK-2: Comparative analysis of Recombinant human IKK-i, TBK-1, and IKK-2. Journal of Biological Chemistry, 277(16), 13840–13847. https://doi.org/10.1074/jbc.M110474200
Larabi, A., Devos, J. M., Ng, S. L., Nanao, M. H., Round, A., Maniatis, T., et al. (2013). Crystal structure and mechanism of activation of TANK-binding kinase 1. Cell Reports, 3(3), 734–746. https://doi.org/10.1016/j.celrep.2013.01.034
Li, F., Xie, X., Wang, Y., Liu, J., Cheng, X., Guo, Y., et al. (2016). Structural insights into the interaction and disease mechanism of neurodegenerative disease-associated optineurin and TBK1 proteins. Nature Communications, 7, Article 12708. https://doi.org/10.1038/ncomms12708
Article PubMed PubMed Central Google Scholar
Ling, L., Cao, Z., & Goeddel, D. V. (1998). NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176. Proc Natl Acad Sci U S A, 95(7), 3792–3797. https://doi.org/10.1073/pnas.95.7.3792
Article PubMed PubMed Central Google Scholar
Lougheed, J. C., Chen, R. H., Mak, P., & Stout, T. J. (2004). Crystal structures of the phosphorylated and unphosphorylated kinase domains of the Cdc42-associated tyrosine kinase ACK1. Journal of Biological Chemistry, 279(42), 44039–44045. https://doi.org/10.1074/jbc.M406703200
Lu, Y., Almeida, S., & Gao, F. B. (2021). TBK1 haploinsufficiency in ALS and FTD compromises membrane trafficking. Acta Neuropathologica, 142(1), 217–221. https://doi.org/10.1007/s00401-021-02331-1
Article PubMed PubMed Central Google Scholar
Maruyama, H., Morino, H., Ito, H., Izumi, Y., Kato, H., Watanabe, Y., et al. (2010). Mutations of optineurin in amyotrophic lateral sclerosis. Nature, 465(7295), 223–226. https://doi.org/10.1038/nature08971
Oakes, J. A., Davies, M. C., & Collins, M. O. (2017). TBK1: A new player in ALS linking autophagy and neuroinflammation. Molecular Brain, 10(1), Article 5. https://doi.org/10.1186/s13041-017-0287-x
Article PubMed PubMed Central Google Scholar
Peters, O. M., Ghasemi, M., & Brown, R. H. Jr. (2015). Emerging mechanisms of molecular pathology in ALS. J Clin Invest, 125(5), 1767–1779. https://doi.org/10.1172/JCI71601
Article PubMed PubMed Central Google Scholar
Pottier, C., Bieniek, K. F., Finch, N., van de Vorst, M., Baker, M., Perkersen, R., et al. (2015). Whole-genome sequencing reveals important role for TBK1 and OPTN mutations in frontotemporal lobar degeneration without motor neuron disease. Acta Neuropathologica, 130(1), 77–92. https://doi.org/10.1007/s00401-015-1436-x
Article PubMed PubMed Central Google Scholar
Reinhardt, R., & Leonard, T. A. (2023). A critical evaluation of protein kinase regulation by activation loop autophosphorylation. eLife. https://doi.org/10.7554/eLife.88210
Article PubMed PubMed Central Google Scholar
Renton, A. E., Majounie, E., Waite, A., Simon-Sanchez, J., Rollinson, S., Gibbs, J. R., et al. (2011). A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron, 72(2), 257–268. https://doi.org/10.1016/j.neuron.2011.09.010
Article PubMed PubMed Central Google Scholar
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., et al. (1993). Mutations in Cu/Zn superoxide dismutase gene are associated with Familial amyotrophic lateral sclerosis. Nature, 362(6415), 59–62. https://doi.org/10.1038/362059a0
Runde, A. P., Mack, R., S, J. P., & Zhang, J. (2022). The role of TBK1 in cancer pathogenesis and anticancer immunity. Journal of Experimental & Clinical Cancer Research : Cr, 41(1), 135. https://doi.org/10.1186/s13046-022-02352-y
Article PubMed Central Google Scholar
Sacks, B., Bashford, J., Wijesekera, L., Leigh, P. N., & Sreedharan, J. (2022). Motor neuron disease: Amyotrophic lateral sclerosis. In D. W. Pfaff, N. D. Volkow, & J. L. Rubenstein (Eds.), Neuroscience in the 21st century: From basic to clinical (pp. 4221–4271). Springer International Publishing.
Sayers, E. W., Beck, J., Bolton, E. E., Brister, J. R., Chan, J., Comeau, D. C., et al. (2024). Database resources of the National Center for Biotechnology Information. Nucleic Acids Research, 52(D1), D33–D43. https://doi.org/10.1093/nar/gkad1044
Sehnal, D., Bittrich, S., Deshpande, M., Svobodova, R., Berka, K., Bazgier, V., et al. (2021). Mol* viewer: Modern web app for 3D visualization and analysis of large biomolecular structures. Nucleic Acids Research, 49(W1), W431–W437. https://doi.org/10.1093/nar/gkab314
Article PubMed PubMed Central Google Scholar
Shao, W., Todd, T. W., Wu, Y., Jones, C. Y., Tong, J., Jansen-West, K., et al. (2022). Two FTD-ALS genes converge on the endosomal pathway to induce TDP-43 pathology and degeneration. Science, 378(6615), 94–99. https://doi.org/10.1126/science.abq7860
Comments (0)