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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.
A broader phenotypic range may be associated with TBK1 copy-number variations, although mutations in this gene are most often detected in patients with normal-tension glaucoma.
Autoubiquitination of TRIM26 (show TRIM26 Proteins) links TBK1 to NEMO (show IKBKG Proteins) in RLR (show DHX58 Proteins)-mediated innate antiviral immune response
ALS (show IGFALS Proteins)-linked mutations in OPTN (show OPTN Proteins) and TBK1 can interfere with mitophagy, suggesting that inefficient turnover of damaged mitochondria may represent a key pathophysiological mechanism contributing to neurodegenerative disease.
Mutations in the TBK1 gene were identified to cause amyotrophic lateral sclerosis (ALS)
In combination with phosphorylation of S177 and S513, this posttranslational modification promotes recruitment and retention of OPTN (show OPTN Proteins)/TBK1 on ubiquitinated, damaged mitochondria
TBK1 should thus also be sequenced, after exclusion of C9orf72 (show C9ORF72 Proteins) mutation, in patients presenting frontotemporal dementia, particularly in cases secondarily associated with amyotrophic lateral sclerosis
TBK1 carriers with amyotrophic lateral sclerosis had shorter disease duration than carriers with frontotemporal dementia in a Belgian cohort.
The expression of TBK1 in mammalian cell mitosis is reported, including localization of the protein during division and its binding properties.
Optineurin (show OPTN Proteins) and TANK-binding kinase 1 (TBK1) are transiently recruited to the polyubiquitinated mitochondria, and the activated TBK1 phosphorylates p62 (show GTF2H1 Proteins) at S403
TBK1 loss of function mutations are the third most frequent cause of clinical frontotemporal dementia in a Belgian cohort.
Innate immune responses to adenovirus vectors are largely TBK1-dependent in the spleen but TBK1-independent in the liver
Data show that the formation of a tripartite ribosomal protein S6 kinase 1 (S6K1 (show RPS6KB1 Proteins))-STING membrane protein-TANK-binding kinase 1 (TBK1) complex was necessary for the activation of interferon regulatory factor-3 (IRF3 (show IRF3 Proteins)).
This study suggest that TBK1 exerts pronociceptive effects in inflammatory nociception which are due to both modulation of NF-kappaB dependent genes and regulation of MAPKs and c-fos.
TRIM27 (show RFP Proteins) inhibits VSV infection-induced type I IFN production by promoting TBK1 degradation.
Suggest that by reducing production of cAMP in adipocytes, PDE3B, IKKepsilon (show IKBKE Proteins) and TBK1 may contribute to the repression of energy expenditure during obesity.
TBK1 has a role in regulating T-cell activation and migration
findings demonstrate a novel regulatory circuit in which STING and TBK1 reciprocally regulate each other to enable efficient antiviral signaling activation, and PPM1A (show PPM1A Proteins) dephosphorylates STING and TBK1
our results identify CK2 (show CSNK2A1 Proteins) as a novel regulator of TBK1 and IRF3 (show IRF3 Proteins) and suggest that targeting CK2 (show CSNK2A1 Proteins) by small molecular inhibitor may be a viable approach to prevent and treat viral infections.
A role for APPL1 (show APPL1 Proteins) in TLR3 (show TLR3 Proteins)/4-dependent TBK1 and IKKepsilon (show IKBKE Proteins) activation in macrophages.
The results highlight the importance of the C-terminal region in the functional activity of IKKepsilon (show IKBKE Proteins) in innate immune response.Interestingly, corresponding region and residues are not required for activation of downstream signaling by TBK1.
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