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this study shows that STAT6 (show STAT6 Proteins) negatively regulates IFNphi1 production by attenuating the kinase activity of TANK-binding kinase 1
Fish IRF6 (show IRF6 Proteins) is distinguished from the homolog of mammals by being a positive regulator of IFN transcription and phosphorylated by MyD88 (show MYD88 Proteins) and TBK1, suggesting that differences in the IRF6 (show IRF6 Proteins) regulation pattern exist between lower and higher vertebrates.
Given the critical roles of TBK1, important regulatory mechanisms are required to regulate its activity. Among these, Optineurin (Optn (show OPTN Proteins)) was shown to negatively regulate the interferon (show IFNA Proteins) response, in addition to its important role in membrane trafficking, protein secretion, autophagy and cell division.
we detected no statistical difference in age at diagnosis or maximum IOP when we compared patients with a TBK1 gene duplication and patients with a TBK1 gene triplication.
Human T-lymphotropic virus 1 Tax (show CNTN2 Proteins) protein impairs K63-linked ubiquitination of STING and disrupted the interactions between STING and TBK1 to evade host innate immunity.
we investigated a large European study population of 2,538 European FTD (show FTL Proteins)-ALS (show IGFALS Proteins) spectrum patients to get a deeper appreciation of the mutation frequency, mutation spectrum, and the genotype-phenotype profile of TBK1 patient carriers.
These results outline a novel mechanism for the control of TBK1 activity and suggest USP1 (show USP1 Proteins)-UAF1 (show WDR48 Proteins) complex as a potential target for the prevention of viral diseases.
TRIM9s undergoes Lys (show LYZ Proteins)-63-linked auto-polyubiquitination and serves as a platform to bridge GSK3beta to TBK1, leading to the activation of IRF3 (show IRF3 Proteins) signaling.
YPEL5 silencing enhanced the induction of IFNB1 (show IFNB1 Proteins) by pattern recognition receptors and phosphorylation of TBK1/IKBKE (show IKBKE Proteins) kinases, whereas co-immunoprecipitation experiments revealed that YPEL5 interacted physically with IKBKE (show IKBKE Proteins).
ZIKV infection of neuroepithelial stem cells and radial glial cells causes centrosomal depletion and mitochondrial sequestration of phospho-TBK1 during mitosis.
High TBK1 expression is associated with Lung cancer.
Our results highlight an unexpected role of the Golgi apparatus in innate immunity as a key subcellular gateway for TBK1 activation after RNA virus infection.
IL-17 (show IL17A Proteins) inhibits adipogenesis where a lack of IL-17 (show IL17A Proteins) ameliorates glucose metabolism. As well, the inhibition of TBK1 reduces inflammation induced by IL-17 (show IL17A Proteins). Therefore, IL-17 (show IL17A Proteins) may be involved in the development of obesity and metabolic dysfunction in a TBK1-dependent manner.
Data show that TBK1 directly interacts with Exo84 (show EXO84 Proteins) through the coiled-coil domain of TBK1 and helical domain of Exo84 (show EXO84 Proteins), and knockdown of TBK1 blocked insulin (show INS Proteins)-stimulated glucose uptake and GLUT4 (show SLC2A4 Proteins) translocation.
The TBK1 Y179A mutant failed to rescue type I IFN production by virally infected RAW264.7 macrophages deficient in TBK1
HERP (show HERPUD1 Proteins) Binds TBK1 To Activate Innate Immunity and Repress Virus Replication in Response to Endoplasmic Reticulum Stress
these studies reveal an additional regulatory function of TRIM8 (show TRIM8 Proteins) in innate immune responses: TRIM8 (show TRIM8 Proteins) catalyzes polyubiquitination of TRIF (show RNF138 Proteins), resulting in disruption of TRIF (show RNF138 Proteins)-TBK1 interaction
TBK1 regulates p16 expression and retinal ganglion cell senescence.
USP38 inhibits type I interferon signaling by editing TBK1 ubiquitination through NLRP4 signalosome.
The authors report that Raf kinase inhibitory protein (RKIP (show PEBP1 Proteins)) is essential for TBK1 activation and type I interferon (show IFNA Proteins) production triggered by viral infection.
Upon stimulation with poly(I:C), malaria parasite-infected red blood cells (iRBCs), or vesicular stomatitis virus (VSV), FOSL1 (show FOSL1 Proteins) "translocated" from the nucleus to the cytoplasm, where it inhibited the interactions between TNF receptor-associated factor 3 (TRAF3 (show TRAF3 Proteins)), TIR domain-containing adapter inducing IFN-beta (show IFNB1 Proteins) (TRIF (show RNF138 Proteins)), and Tank-binding kinase 1 (TBK1) via impairing K63-linked polyubiquitination of TRAF3 (show TRAF3 Proteins) and TRIF (show RNF138 Proteins).
TBK1 complexes required for the phosphorylation of IRF3 (show IRF3 Proteins) and the production of interferon-beta (show IFNB1 Proteins) have been identified.
The NF-kappa-B (NFKB) complex of proteins is inhibited by I-kappa-B (IKB) proteins, which inactivate NFKB by trapping it in the cytoplasm. Phosphorylation of serine residues on the IKB proteins by IKB kinases marks them for destruction via the ubiquitination pathway, thereby allowing activation and nuclear translocation of the NFKB complex. The protein encoded by this gene is similar to IKB kinases and can mediate NFKB activation in response to certain growth factors.
serine/threonine-protein kinase TBK1
, TANK-binding kinase 1
, NF-kappa-B-activating kinase
, TANK binding kinase 1
, serine/threonine protein kinase TBK1
, serine/threonine-protein kinase TBK1-like
, NF-kB-activating kinase