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Adaptor-Mediated Trafficking of Tank Binding Kinase 1 During Diverse Cellular Processes.

Title: Adaptor-Mediated Trafficking of Tank Binding Kinase 1 During Diverse Cellular Processes.
Authors: Paul S; Graduate Program in Biomedical and Veterinary Sciences, Virginia-Maryland College of Veterinary Medicine, Blacksburg, Virginia, USA.; Biswas SR; Translational Biology, Medicine, and Health Graduate Program, Virginia Polytechnic Institute and State University, Roanoke, Virginia, USA.; Milner JP; School of Neuroscience, Virginia Polytechnic Institute and State University, Blacksburg, Virginia, USA.; Tomsick PL; School of Neuroscience, Virginia Polytechnic Institute and State University, Blacksburg, Virginia, USA.; Pickrell AM; School of Neuroscience, Virginia Polytechnic Institute and State University, Blacksburg, Virginia, USA.
Source: Traffic (Copenhagen, Denmark) [Traffic] 2025 Jan-Mar; Vol. 26 (1-3), pp. e70000.
Publication Type: Journal Article; Review
Language: English
Journal Info: Publisher: Wiley Country of Publication: England NLM ID: 100939340 Publication Model: Print Cited Medium: Internet ISSN: 1600-0854 (Electronic) Linking ISSN: 13989219 NLM ISO Abbreviation: Traffic Subsets: MEDLINE
Imprint Name(s): Publication: Oxford : Wiley; Original Publication: Copenhagen, Denmark ; Malden, MA : Munksgaard, c2000-
MeSH Terms: Protein Serine-Threonine Kinases*/metabolism ; Adaptor Proteins, Signal Transducing*/metabolism; Protein Transport/physiology ; Humans ; Animals ; Signal Transduction ; Cell Cycle Proteins ; Protein Binding ; Autophagy ; Membrane Transport Proteins
Abstract: The serine/threonine kinase, Tank Binding Kinase 1 (TBK1), drives distinct cellular processes like innate immune signaling, selective autophagy, and mitosis. It is suggested that the translocation and activation of TBK1 at different subcellular locations within the cell, downstream of diverse stimuli, are driven by TBK1 adaptor proteins forming a complex directly or indirectly with TBK1. Various TBK1 adaptors and associated proteins like NAP1, TANK, SINTBAD, p62, optineurin (OPTN), TAX1BP1, STING, and NDP52 have been identified in facilitating TBK1 activation and recruitment with varying overlapping redundancy. This review focuses on what is known about these proteins, their interactions with TBK1, and the functional consequences of these associations. We shed light on underexplored areas of research on these TBK1 binding partners while emphasizing how future research is required to understand the function and flexibility of TBK1 signaling and crosstalk or regulation between different biological processes.; (© 2025 The Author(s). Traffic published by John Wiley & Sons Ltd.)
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Grant Information: R35 GM142368 United States GM NIGMS NIH HHS; United States NH NIH HHS
Contributed Indexing: Keywords: NAP1; NDP52; OPTN; SINTBAD; TANK; TAX1BP1; TBK1; autophagy; innate immunity; p62
Substance Nomenclature: EC 2.7.11.1 (Protein Serine-Threonine Kinases); EC 2.7.11.1 (TBK1 protein, human); 0 (Adaptor Proteins, Signal Transducing); 0 (Cell Cycle Proteins); 0 (OPTN protein, human); 0 (Membrane Transport Proteins)
Entry Date(s): Date Created: 20250306 Date Completed: 20250511 Latest Revision: 20260127
Update Code: 20260130
PubMed Central ID: PMC11883510
DOI: 10.1111/tra.70000
PMID: 40047067
Database: MEDLINE

Journal Article; Review