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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.
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.
The results of this study proposed that TBK1 is not a frequent causal gene in Chinese ALS patients.
HERP (show HERPUD1 Proteins) Binds TBK1 To Activate Innate Immunity and Repress Virus Replication in Response to Endoplasmic Reticulum Stress
these data suggest that HNSs, an antagonist of host innate immunity, interacts with TBK1 and thereby hinders the association of TBK1 with its substrate IRF3 (show IRF3 Proteins), thus blocking IRF3 (show IRF3 Proteins) activation and transcriptional induction of the cellular antiviral responses.
Pathogenic variants in TBK1 are rare but could be responsible for sALS (show CDH23 Proteins) in a small number of Korean patients.
High TBK1 expression is associated with normal tension glaucoma.
We identified novel genomic TBK1 variants including two loss-of-function (LoF) (p.Leu59Phefs*16 and c.358+5G>A), two missense (p.Asp118Asn and p.Ile397Thr) and one intronic variant (c.1644-5_1644-2delAATA).
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
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.
this study reveals a previously unknown ICOS (show ICOS Proteins)-TBK1 signaling pathway that specifies the commitment of germinal center follicular helper T cells
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