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GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression[ChIP-seq]

ABSTRACT: GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression[ChIP-seq]

PROVIDER: PRJNA836799 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR19154665_1.fastq.gz	Fastqsanger.gz
	SRR19154665_2.fastq.gz	Fastqsanger.gz
	SRR19154666_1.fastq.gz	Fastqsanger.gz
	SRR19154666_2.fastq.gz	Fastqsanger.gz
	SRR19154667_1.fastq.gz	Fastqsanger.gz

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GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression[ChIP-seq]

Project description:Phosphorylation of estrogen receptor α (ER) at serine 118 (pS118-ER) is induced by estrogen and is the most abundant post-translational mark associated with a transcriptionally active receptor. Cistromic analysis of pS118-ER from our group found enrichment of the GRHL2 motif near pS118-ER binding sites. In this report we use cistromic and transcriptomic analyses to interrogate the relationship between GRHL2 and pS118-ER. We found that GRHL2 is bound to chromatin at pS118-ER/GRHL2 co-occupancy sites prior to ligand treatment, and GRHL2 binding is required for maximal pS118-ER recruitment. pS118-ER/GRHL2 co-occupancy sites were enriched at active enhancers marked by H3K27ac and H3K4me1, along with FOXA1 and p300. Transcriptomic analysis yielded four subsets of ER/GRHL2 co-regulated genes revealing that GRHL2 can both enhance and antagonize E2-mediated ER transcriptional activity. Gene ontology analysis identified several coregulated genes involved in cell migration. Accordingly, knockdown of GRHL2 combined with estrogen treatment resulted in increased cell migration but no change in proliferation. These results support a model in which GRHL2 binds to select enhancers and facilitates pS118-ER recruitment to chromatin which then results in differential activation and repression of genes that control ER-positive breast cancer cell migration.

2022-05-19 | GSE202620 | GEO

GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression [Cut&Run]

2022-05-19 | GSE202619 | GEO

GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression [RNA-seq]

2022-05-19 | GSE202621 | GEO

GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression

Project description:GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression

| PRJNA836788 | ENA

GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression [Cut&Run]

Project description:GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression [Cut&Run]

| PRJNA836800 | ENA

GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression [RNA-seq]

Project description:GRHL2 enhances phosphorylated estrogen receptor DNA binding and regulates ER-mediated transcriptional activation and repression [RNA-seq]

| PRJNA836798 | ENA

Analysis of the Phosphorylated Estrogen Receptor-α Cistrome Reveals Association with Direct ER-DNA Binding and the Transcription Factor GRHL2

Project description:Phosphorylation of the estrogen receptor-α (ER) at serine 118 (pS118-ER) is involved in modulating ER-dependent gene transcription and recruitment of ER to certain gene promoters. While the effects of pS118 on ER-DNA interactions have been investigated at specific sites, the genome-wide binding profile (cistrome) of pS118-ER remains to be studied. To characterize the pS118-ER cistrome, ChIP-seq was performed on pS118-ER and pan-ER in MCF-7 cells. A subset of ER sites was occupied by pS118-ER and these sites were associated with the active enhancer mark H3K27ac. Additionally, pS118-ER sites were found to be enriched in the DNA binding motif for GRHL2 as well as the estrogen response element relative to all ER sites. Utilizing a DNA binding microarray, pS118-ER was found to be more commonly associated with direct DNA binding events compared to indirect binding events. These results suggest a role for pS118-ER at active enhancers and as a regulator of direct ER-DNA interactions.

2018-12-11 | GSE117569 | GEO

Elevated GRHL2 imparts plasticity in estrogen receptor positive breast cancer cells [ChIP-Seq]

Project description:Estrogen receptor (ER) positive breast cancer is characterized by a late recurrence following initial treatment. The epithelial cell fate transcription factor Grainyhead-like protein 2 (GRHL2) is amplified in ER positive breast cancers and is indicative of poorer prognosis as compared to ER negative breast cancer. To understand how GRHL2 contributes to progression, GRHL2 was overexpressed in ER positive cells. To determine how GRHL2 overexpression affects GRHL2 binding to DNA, ChIP sequencing was conducted to evaluate binding intensity and location.

2024-08-25 | GSE272059 | GEO

Elevated GRHL2 imparts plasticity in estrogen receptor positive breast cancer cells [RNA-seq]

Project description:Estrogen receptor (ER) positive breast cancer is characterized by a late recurrence following initial treatment. The epithelial cell fate transcription factor Grainyhead-like protein 2 (GRHL2) is amplified in ER positive breast cancers and is indicative of poorer prognosis as compared to ER negative breast cancer. To understand how GRHL2 contributes to progression, GRHL2 was overexpressed in ER positive cells. To examine gene expression changes from elevated GRHL2 levels, RNA-sequencing was performed to better comprehend how high GRHL2 may change its transcriptional activity.

2024-08-25 | GSE272061 | GEO

GRHL2 Enhances Phosphorylated Estrogen Receptor (ER) Chromatin Binding and Regulates ER-Mediated Transcriptional Activation and Repression.

Project description:Phosphorylation of estrogen receptor α (ER) at serine 118 (pS118-ER) is induced by estrogen and is the most abundant posttranslational mark associated with a transcriptionally active receptor. Cistromic analysis of pS118-ER from our group revealed enrichment of the GRHL2 motif near pS118-ER binding sites. In this study, we used cistromic and transcriptomic analyses to interrogate the relationship between GRHL2 and pS118-ER. We found that GRHL2 is bound to chromatin at pS118-ER/GRHL2 co-occupancy sites prior to ligand treatment, and GRHL2 binding is required for maximal pS118-ER recruitment. pS118-ER/GRHL2 co-occupancy sites were enriched at active enhancers marked by H3K27ac and H3K4me1, along with FOXA1 and p300, compared to sites where each factor binds independently. Transcriptomic analysis yielded four subsets of ER/GRHL2-coregulated genes revealing that GRHL2 can both enhance and antagonize E2-mediated ER transcriptional activity. Gene ontology analysis indicated that coregulated genes are involved in cell migration. Accordingly, knockdown of GRHL2, combined with estrogen treatment, resulted in increased cell migration but no change in proliferation. These results support a model in which GRHL2 binds to selected enhancers and facilitates pS118-ER recruitment to chromatin, which then results in differential activation and repression of genes that control estrogen-regulated ER-positive breast cancer cell migration.

| S-EPMC9584124 | biostudies-literature

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