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Phosphorylation of AGO2 by TBK1 Promotes the Formation of Oncogenic miRISC in NSCLC

ABSTRACT: Phosphorylation of AGO2 by TBK1 Promotes the Formation of Oncogenic miRISC in NSCLC

PROVIDER: PRJNA940667 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR23693745_1.fastq.gz	Fastqsanger.gz
	SRR23693745_2.fastq.gz	Fastqsanger.gz
	SRR23693746_1.fastq.gz	Fastqsanger.gz
	SRR23693746_2.fastq.gz	Fastqsanger.gz
	SRR23693747.fastq.gz	Fastqsanger.gz

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Phosphorylation of AGO2 by TBK1 Promotes the Formation of Oncogenic miRISC in NSCLC

Project description:Non-small-cell lung cancer (NSCLC) is a highly lethal tumor that often develops resistance to targeted therapy. It is shown that Tank-binding kinase 1 (TBK1) phosphorylates AGO2 at S417 (pS417-AGO2), which promotes NSCLC progression by increasing the formation of microRNA-induced silencing complex (miRISC). High levels of pS417-AGO2 in clinical NSCLC specimens are positively associated with poor prognosis. Interestingly, the treatment with EGFR inhibitor Gefitinib can significantly induce pS417-AGO2, thereby increasing the formation and activity of oncogenic miRISC, which may contribute to NSCLC resistance to Gefitinib. Based on these, two therapeutic strategies is developed. One is jointly to antagonize multiple oncogenic miRNAs highly expressed in NSCLC and use TBK1 inhibitor Amlexanox reducing the formation of oncogenic miRISC. Another approach is to combine Gefitinib with Amlexanox to inhibit the progression of Gefitinib-resistant NSCLC. This findings reveal a novel mechanism of oncogenic miRISC regulation by TBK1-mediated pS417-AGO2 and suggest potential therapeutic approaches for NSCLC.

2024-03-03 | GSE226548 | GEO

Phosphorylation of AGO2 by TBK1 Promotes the Formation of Oncogenic miRISC in NSCLC.

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TBK1-mediated LC3C phosphorylation site identification

Project description:In order to identify TBK1-mediated LC3C phosphorylation sites, proteins were overexpressed in SILAC labelled cells.

2019-11-06 | PXD015076 | Pride

endogenous TBK1-mediated GABARAP-L2 and LC3C phosphorylation site identification

Project description:In order to identify TBK1-mediated GABARAP-L2 and LC3C phosphorylation sites, cells were treated with TBK1 or control siRNA and TBK1 kinase activity was induced by treatment with CCCP.

2019-11-06 | PXD015077 | Pride

Transcription profiling of immortalized human lung epithelial cells following oncogenic KRAS expression and TBK1 suppression

Project description:The purpose of the dataset is to analyze expression of genes induced by KRAS and regulated by TBK1; The proto-oncogene KRAS is mutated in a wide array of human cancers, most of which are aggressive and respond poorly to standard therapies. Although the identification of specific oncogenes has led to the development of clinically effective, molecularly targeted therapies in some cases, KRAS has remained refractory to this approach. An alternative strategy for targeting KRAS is to identify gene products that, when suppressed or inhibited, result in cell death only in the presence of an oncogenic allele. Here we have used systematic RNA interference (RNAi) to detect synthetic lethal partners of oncogenic KRAS and found that the non-canonical IkB kinase, TBK1, was selectively essential in cells that harbor mutant KRAS. Suppression of TBK1 induced apoptosis specifically in human cancer cell lines that depend on oncogenic KRAS expression. In these cells, TBK1 activated NF- B anti-apoptotic signals involving cREL and BCL-XL that were essential for survival, providing mechanistic insights into this synthetic lethal interaction. These observations identify TBK1 as a potential therapeutic target in KRAS mutant tumors and establish a general approach for the rational identification of co-dependent pathways in cancer. Experiment Overall Design: Knock out of TBK1 in the contect of KRAS activation (mutant) and control (WT)

2009-11-15 | E-GEOD-17643 | biostudies-arrayexpress

TBK1-mediated GABARAP-L2 phosphorylation site identification

Project description:In order to identify TBK1-mediated GABARAP-L2 phosphorylation sites, proteins were overexpressed in SILAC labelled cells.

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The phosphorylation of TBK1

Project description:Explore the phosphorylation sites of TBK1 whick is modified by AKT1.

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Transcription profiling of human lung epithelial cells ollowing oncogenic KRAS expression and TBK1 suppression or infection with oncogenic KRAS (G12V) - SuperSeries

Project description:The proto-oncogene KRAS is mutated in a wide array of human cancers, most of which are aggressive and respond poorly to standard therapies. Although the identification of specific oncogenes has led to the development of clinically effective, molecularly targeted therapies in some cases, KRAS has remained refractory to this approach. An alternative strategy for targeting KRAS is to identify gene products that, when suppressed or inhibited, result in cell death only in the presence of an oncogenic allele. Here we have used systematic RNA interference (RNAi) to detect synthetic lethal partners of oncogenic KRAS and found that the non-canonical IkB kinase, TBK1, was selectively essential in cells that harbor mutant KRAS. Suppression of TBK1 induced apoptosis specifically in human cancer cell lines that depend on oncogenic KRAS expression. In these cells, TBK1 activated NF- B anti-apoptotic signals involving cREL and BCL-XL that were essential for survival, providing mechanistic insights into this synthetic lethal interaction. These observations identify TBK1 as a potential therapeutic target in KRAS mutant tumors and establish a general approach for the rational identification of co-dependent pathways in cancer. This SuperSeries is composed of the following subset Series:; GSE17643: Profiling of immortalized human lung epithelial cells following oncogenic KRAS expression and TBK1 suppression; GSE17671: Profiling of immortalized human lung epithelial cells following infection with oncogenic KRAS (G12V) Experiment Overall Design: Refer to individual Series

2009-10-31 | E-GEOD-17672 | biostudies-arrayexpress

Precipitation of mRNAs by Ago2 and phosphorylation mutants

Project description:Argonaute (Ago) proteins associate with microRNAs (miRNAs), which guide them to complementary target mRNAs resulting in gene silencing. RNA coimmunoprecipitations (RIP) were performed with Ago2 and Ago2 mutants. The precipitated mRNAs were analyzed using one Affymetrix microarrays to compare the mRNA preciptation rates of mutants vs Ago2 wild type.

2017-06-22 | GSE92698 | GEO

hnRNPM, ELAVL1, and TBK1 form a type I interferon-inducing multiprotein complex downstream of cGAS and RIG-I

Project description:RIG-I like helicases (RLHs) and cGAS are crucial cytosolic sensors of viral RNA and DNA, respectively, and induce type I IFNs via TBK1/IKKε. hnRNPM was described to possess antimicrobial activities. Here, we show that hnRNPM promotes TBK1/IRF3 phosphorylation and type I IFN induction downstream of cGAS and RIG-I in THP-1 cells and primary human fibroblasts. Interactome analysis revealed that hnRNPM forms a multiprotein complex with ELAVL1, SON, TBK1, IKKε, IKKβ, and NF-κB p65. The purified hnRNPM complex enhanced TBK1 phosphorylation. Vice versa, TBK1 directly phosphorylated ELAVL1. hnRNPM, ELAVL1, and TBK1 predominantly interacted in the cytosol. Of note, patients with mutations in SON suffer from recurrent infections, further underlining its biologic significance. To our knowledge, hnRNPM, ELAVL1, and SON represent the first non-redundant signaling components merging the cGAS-STING and RIG-I–MAVS pathways. Therefore, our findings may have implications for host defense and auto-inflammatory diseases.

2023-09-16 | GSE184273 | GEO

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