Synopsis
Originally discovered as a kinase that interacted with the effector proteins TANK and TRAF2 in a ternary complex that could activate NF-κB, TANK-binding kinase 1 (TBK1) has since been characterized as a key regulator of substrates ranging from cell proliferation and vesicle transport to xenophagic elimination of bacteria and antiviral immune response. Also known as NAK (NF-κB-activating kinase) or T2K (TRAF2-associated kinase), TBK1 is a ubiquitously expressed 729-amino-acid serine/threonine kinase that is a noncanonical IκB kinase family member, targeting the transcription factors IRF3 and IRF7 in the type I interferon response. TBK1 is composed of an N-terminal kinase domain (KD), which contains an activation loop between subdomains VII and VIII controlling its catalytic activity, and three C-terminal regulatory domains: a ubiquitin-like domain (ULD), which interacts with the KD rather than the known ubiquitin-binding proteins and appears to be necessary for substrate...
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Marion, J. (2018). TANK-Binding Kinase 1 (TBK1): Structure, Function, and Regulation. In: Wells, R.D., Bond, J.S., Klinman, J., Masters, B.S.S. (eds) Molecular Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1531-2_374
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DOI: https://doi.org/10.1007/978-1-4614-1531-2_374
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