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Heat Shock Factor 1 (HSF1) supports the ESR1 action in breast cancer (ChIP-seq)

ABSTRACT: Heat Shock Factor 1 (HSF1) supports the ESR1 action in breast cancer (ChIP-seq)

PROVIDER: PRJNA670336 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12855324.fastq.gz	Fastqsanger.gz
	SRR12855325.fastq.gz	Fastqsanger.gz
	SRR12855326.fastq.gz	Fastqsanger.gz
	SRR12855327.fastq.gz	Fastqsanger.gz
	SRR12855328.fastq.gz	Fastqsanger.gz

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Heat Shock Factor 1 (HSF1) supports the ESR1 action in breast cancer

Project description:Heat Shock Factor 1 (HSF1) supports the ESR1 action in breast cancer

| PRJNA670490 | ENA

Heat Shock Factor 1 (HSF1) supports the ESR1 action in breast cancer (ChIP-seq)

Project description:Heat shock factor 1 (HSF1) is a key regulator of transcriptional responses to proteotoxic stress. It has been recently linked to signaling of estrogen via ESR1. To study the cooperation of HSF1 and ESR1 in the transcriptional response to estrogen, we established estrogen receptor (ER)-positive breast cancer cell lines with reduced HSF1 levels using specific shRNA or CRISPR/Cas9 approach. HSF1 deficiency led to the inhibition of the mitogenic effect of estrogen in MCF7 and T47D cells. RNA-seq analyses revealed that the stimulatory effect of E2 on the transcriptome was smaller in HSF1-deficient MCF7 cells. This could partially result from the higher basal expression of E2-dependent genes in these cells as a consequence of the enhanced binding of unliganded ESR1 to chromatin, which was revealed by ChIP-seq analyses. Thus, we postulate that some fraction of ESR1 could be released from the inhibitory complex with HSP90 and gain transcriptional competence without E2-stimulation.

2021-10-21 | GSE159724 | GEO

Heat Shock Factor 1 (HSF1) supports the ESR1 action in breast cancer (RNA-seq)

2021-10-19 | GSE159802 | GEO

Heat Shock Factor 1 (HSF1) supports the ESR1 action in breast cancer (RNA-seq)

Project description:Heat Shock Factor 1 (HSF1) supports the ESR1 action in breast cancer (RNA-seq)

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Heat Shock Factor 1 (HSF1) regulates ESR1 action in breast cancer

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Heat Shock Factor 1 (HSF1) regulates ESR1 action in breast cancer

Project description:Heat Shock Factor 1 (HSF1) regulates ESR1 action in breast cancer

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HSF1 Mouse Fibroblast Heat Shock - Scanner7

Project description:Mouse HSF1+/+ and HSF1-/- Fibroblasts Heat Shock Time Courses Scanned on Scanner 7 (Axon 4000B) Set of arrays organized by shared biological context, such as organism, tumors types, processes, etc. Keywords: Logical Set

2005-08-05 | GSE3074 | GEO

Transcription profiling of mouse HSF1+/+ and HSF1-/- fibroblasts heat shock time series

Project description:Mouse HSF1+/+ and HSF1-/- Fibroblasts Heat Shock Time Courses Scanned on Scanner 7 (Axon 4000B)

2005-07-21 | E-SMDB-1853 | biostudies-arrayexpress

Heat Shock Factor 1 (HSF1) supports the ESR1 action in breast cancer

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

2021-10-20 | GSE159803 | GEO

HSF1 and HSF2 interactions with chromatin during the heat shock response in mouse spermatocytes

Project description:Heat shock transcription factors HSF1 and HSF2 both are necessary for proper spermatogenesis, which is disrupted at elevated temperatures. We studied how HSF1 and HSF2 cooperate during the heat shock response in mouse spermatocytes. For this purpose we used ChIP-sequencing. ChIP-Seq analyses revealed that the temperature elevation induces remodeling of HSF1 and HSF2 binding to chromatin. The highest HSF1-chromatin binding was observed at 43°C, when HSF2-chromatin binding was reduced. Many promoters (mainly Hsp genes) were occupied by both heat shock factors at physiological temperature of testes and/or at 38°C. In contrary at 43°C only HSF1 was bound. Obtained results suggest that HSF1 and HSF2 could cooperate in regulation of the transcription of some genes only at physiological temperatures and/or at 38°C. Alteration in HSFs interactions and their binding to chromatin could be one of the reason of increased spermatogenic cell death observed after heat shock.

2014-10-07 | GSE56735 | GEO

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