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BET inhibition disrupts transcription but retains enhancer-promoter contact [Capture-C]

ABSTRACT: BET inhibition disrupts transcription but retains enhancer-promoter contact [Capture-C]

PROVIDER: PRJNA579833 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR10352100_1.fastq.gz	Fastqsanger.gz
	SRR10352100_2.fastq.gz	Fastqsanger.gz
	SRR10352101_1.fastq.gz	Fastqsanger.gz
	SRR10352101_2.fastq.gz	Fastqsanger.gz
	SRR10352102_1.fastq.gz	Fastqsanger.gz

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BET inhibition disrupts transcription but retains enhancer-promoter contact

Project description:BET inhibition disrupts transcription but retains enhancer-promoter contact

| PRJNA579830 | ENA

BET inhibition disrupts transcription but retains enhancer-promoter contact [RNA-seq]

Project description:BET inhibition disrupts transcription but retains enhancer-promoter contact [RNA-seq]

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BET inhibition disrupts transcription but retains enhancer-promoter contact [ChIP-seq]

Project description:BET inhibition disrupts transcription but retains enhancer-promoter contact [ChIP-seq]

| PRJNA579832 | ENA

BET inhibition disrupts transcription but retains enhancer-promoter contact [Capture-C]

Project description:Enhancers are DNA sequences that enable complex temporal and tissue-specific regulation of genes in higher eukaryotes. Although it is not entirely clear how enhancer-promoter interactions can increase gene expression, this proximity has been observed in multiple systems at multiple loci and is thought to be essential for the maintenance of gene expression. Bromodomain and Extra-Terminal domain (BET) and Mediator proteins have been shown capable of forming phase condensates and are thought to be essential for super-enhancer function. Here, we show that targeting of cells with inhibitors of BET proteins or pharmacological degradation of BET protein Bromodomain-containing protein 4 (BRD4) has a strong impact on transcription but very little impact on enhancer-promoter interactions. Dissolving phase condensates reduces BRD4 and Mediator binding at enhancers and can also strongly affect gene transcription, without disrupting enhancer-promoter interactions. These results suggest that activation of transcription and maintenance of enhancer-promoter interactions are separable events. Our findings further indicate that enhancer-promoter interactions are not dependent on high levels of BRD4 and Mediator, and are likely maintained by a complex set of factors including additional activator complexes and, at some sites, CTCF and cohesin.

2020-10-26 | GSE139434 | GEO

BET inhibition disrupts transcription but retains enhancer-promoter contact [RNA-seq]

2020-10-26 | GSE139436 | GEO

BET inhibition disrupts transcription but retains enhancer-promoter contact [ChIP-seq]

2020-10-26 | GSE139435 | GEO

BET inhibition disrupts transcription but retains enhancer-promoter contact.

| S-EPMC7801379 | biostudies-literature

BET inhibition disrupts transcription but retains enhancer-promoter contact

Project description:This SuperSeries is composed of the SubSeries listed below.

2020-10-26 | GSE139437 | GEO

BET Bromodomain Degradation Disrupts Function but Not 3D Formation of RNA Pol2 Clusters

Project description:BET Bromodomain Degradation Disrupts Function but Not 3D Formation of RNA Pol2 Clusters

| PRJNA1084004 | ENA

RAPID RESISTANCE TO BET INHIBITORS IS MEDIATED BY FGFR1 IN GLIOBLASTOMA

Project description:Bromodomain and extra-terminal domain (BET) proteins are therapeutic targets in several cancers including the most common malignant adult brain tumor glioblastoma (GBM). Multiple small molecule inhibitors of BET proteins have been utilized in preclinical and clinical studies. Unfortunately, BET inhibitors have not shown efficacy in clinical trials enrolling GBM patients. One possible reason for this may stem from resistance mechanisms that arise after prolonged treatment within a clinical setting. However, the mechanisms and timeframe of resistance to BET inhibitors in GBM is not known. To identify the temporal order of resistance mechanisms in GBM we performed quantitative proteomics using multiplex-inhibitor bead mass spectrometry and demonstrated that resistance to BET inhibitors in GBM treatment occurs rapidly within hours and involves the fibroblast growth factor receptor 1 (FGFR1) protein. Small molecule inhibition of BET proteins and FGFR1 simultaneously induces synergy in reducing GBM tumor growth in vitro and in vivo. Further, FGFR1 knockdown synergizes with BET inhibitor mediated reduction of GBM cell proliferation. Collectively, our studies suggest that co-targeting BET and FGFR1 may dampen resistance mechanisms to yield a clinical response in GBM.

2024-06-16 | PXD043214 | Pride

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