Ask about this productRelated genes to: TBK1 antibody
- Gene:
- TBK1 NIH gene
- Name:
- TANK binding kinase 1
- Previous symbol:
- -
- Synonyms:
- NAK
- Chromosome:
- 12q14.2
- Locus Type:
- gene with protein product
- Date approved:
- 2000-06-08
- Date modifiied:
- 2019-04-23
Related products to: TBK1 antibody
Related articles to: TBK1 antibody
- Bladder cancer (BC), particularly muscle-invasive or metastatic disease, remains a major clinical challenge despite advances in immunotherapy. In this study, five candidate small molecules were screened, and cryptotanshinone (CTS) was identified as the most promising compound. Using BC cell lines and bladder tumor organoids, we evaluated the effects of CTS on proliferation, migration, apoptosis, and organoid growth. Transcriptomic sequencing of bladder tumor organoids, combined with protein-protein interaction analysis and public databases (TCGA-BLCA, TIMER, and TISIDB), was used to characterize CTS-associated molecular features. Integrative analyses identified IFIT1, IFIT2, and IFIT3 as representative interferon-stimulated candidate genes associated with BC progression, prognosis, immune infiltration, and PD-1/PD-L1 expression. These findings were supported by qRT-PCR and Western blot analyses showing reduced IFIT1/2/3 expression at both mRNA and protein levels following CTS treatment. Molecular docking suggested potential associations between CTS and interferon-related signaling proteins. Consistently, CTS reduced TBK1 and STAT1 phosphorylation, providing preliminary experimental support for its association with interferon-related signaling modulation. Collectively, CTS exerts growth-inhibitory effects and is associated with tumor cell-intrinsic interferon-related transcriptional and signaling changes in BC models, providing a basis for further investigation as a small-molecule candidate for BC. - Source: PubMed
Publication date: 2026/05/13
Yang MengniLi ShanLi RuiDong YuZhou MengtingZhao JunningLiu MiaoTan Ruirong - The autophagy-lysosome system directs the degradation of a wide variety of cytoplasmic cargo such as damaged organelles, protein aggregates, and invading pathogens. The autophagy receptor IRGQ harbors two distinct LIR domains, with LIR1 exhibiting high selectivity for GABARAPL2. Proteomic, biochemical, and high-throughput microscopy studies reveal that the IRGQ-GABARAPL2 complex functions as a hub for the interaction between hATG8s and the autophagy initiation machinery, promoting their lipidation and overall autophagic flux. The interaction of IRGQ with GABARAPL2 is regulated via TBK1. Upon TBK1 activation, GABARAPL2 is phosphorylated on S10, which disrupts IRGQ-GABARAPL2 complexation and therefore its interaction with the autophagy initiation machinery, resulting in a reduction of the autophagic flux of GABARAPL2 and IRGQ-cargo, without affecting bulk autophagy. These findings broaden IRGQ's role in autophagy, identifying it as an interaction hub for autophagy initiation that is negatively regulated by TBK1. - Source: PubMed
Publication date: 2026/05/13
Gestal-Mato UxiaLascaux PaulinePoveda-Cuevas Sergio AlejandroCristiani AlbertoCamp BelindaAghapour MahyarAmmanath Aparna ViswanathanBhaskara Ramachandra MDikic IvanHerhaus Lina - Heterogeneous nuclear ribonucleoproteins (hnRNPs) play important roles in the life cycle of influenza A virus (IAV). Our previous mass spectrometry analysis identified cellular hnRNP D as a novel interaction partner of the IAV polymerase basic 2 (PB2) protein. However, the functional implications of hnRNP D in IAV replication and the underlying mechanisms remained unknown. In this study, we confirmed that hnRNP D directly interacts with the PB2 protein of the A/Puerto Rico/8/1934 (PR8, H1N1) strain, while also binding to other proteins within viral ribonucleoprotein complexes (vRNPs). These interactions collectively inhibit vRNPs assembly and viral polymerase activity. However, we have found that hnRNP D enhances the viral titer of IAV in A549 cells. Mechanistically, hnRNP D suppresses the activation of the interferon (IFN)-β promoter, and the mRNA levels of downstream factors in the type I IFN signaling pathway. In detail, hnRNP D inhibits IFN-β promoter activation induced by crucial antiviral proteins and interacts strongly with the interferon regulatory factor 3 (IRF3). More importantly, hnRNP D blocks the binding of TANK-binding kinase 1 (TBK1) to IRF3, thereby impeding the phosphorylation and activation of IRF3. Collectively, we unveil a novel viral immune evasion strategy by which IAV hijacks a host RNA-binding protein, hnRNP D, to facilitate self-replication. This work not only elucidates the intricate trade-off mechanisms in virus-host interaction but also identifies hnRNP D as a potential therapeutic target aimed at bolstering antiviral immunity. - Source: PubMed
Publication date: 2026/05/13
Xu ChenchenPeng YunlingLiu ShuhuiXie RanFeng DuanchenxiBi ZhenweiYan Liping - The innate immune signaling pathway cGAS-STING plays an important role in the recognition of cytosolic nucleic acids and the induction of the interferon-dependent antiviral response. Despite the significant research interest in this cascade in the context of immune system function, the mechanisms regulating cGAS-STING signaling and the switch between its pro-inflammatory and pro-apoptotic effects remain largely underexplored. According to publicly available RNA-seq data and microarray analyses, SETD7 lysine methyltransferase participates in interferon signaling in cancer cells. This study aims to elucidate the role of SETD7 in the regulation of the STING-dependent immune response in human lung adenocarcinoma (LUAD) cells. For this purpose, we developed a reproducible and cost-effective method for inducing the STING cascade by transfecting cells with salmon sperm DNA (sspDNA). We demonstrated that sspDNA efficiently induces phosphorylation of the key components of the STING-TBK1-IRF3 signaling pathway and activates the expression of interferons and pro-inflammatory cytokines. Using this approach, we further demonstrated that SETD7 is involved in the regulation of the IRF3-dependent transcriptional program. Suppression of SETD7 was associated with changes in the expression of genes related to innate immune response and apoptosis, including increased levels of , , , (PUMA), and . Furthermore, attenuation of SETD7 expression reduced the lentiviral transduction efficacy in H1299 cells. These results suggest that SETD7 may play a role in regulating the switch in STING signaling between pro-inflammatory and pro-apoptotic responses in LUAD cells. - Source: PubMed
Publication date: 2026/04/30
Nevzorov Ivan AKorableva PolinaShuvalov OlegParfenyev SergeyBarlev Nickolai ADaks Alexandra - Amyotrophic lateral sclerosis (ALS) is marked by immune dysregulation; however, the role of T cell-ubiquitination-related genes (TURGs) in its pathogenesis remains unclear. This study aimed to investigate the contribution of TURGs to T-cell dysfunction and ubiquitination imbalance in ALS. - Source: PubMed
Publication date: 2026/05/05
Jiang AilingHuang YanzhenQue XiantingLi ChonglinLin ZiqunHuang Wen