Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Neurofibromin is an Estrogen Receptor alpha Transcriptional Co-repressor in Breast cancer

ABSTRACT: Neurofibromin is an Estrogen Receptor alpha Transcriptional Co-repressor in Breast cancer

PROVIDER: PRJNA597127 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Similar Datasets

Neurofibromin is an Estrogen Receptor alpha Transcriptional Co-repressor in Breast cancer

Project description:We report that neurofibromin, a tumor suppressor and Ras-GAP (GTPase Activating Protein), is also an estrogen receptor-alpha (ER) transcriptional co-repressor through leucine/isoleucine-rich motifs that are functionally independent of GAP activity. GAP activity, in turn, does not impact ER binding. Consequently, neurofibromin-depletion causes estradiol hypersensitivity and tamoxifen agonism, explaining the poor prognosis associated with neurofibromin-loss in endocrine therapy-treated ER+ breast cancer. Neurofibromin-deficient ER+ breast cancer cells initially retain sensitivity to selective estrogen receptor degraders (SERDs). However, Ras activation does play a role in acquired SERD resistance, which can be reversed upon MEK inhibitor addition, and SERD/MEK inhibitor combinations induce tumor regression. Thus, neurofibromin is a dual repressor for both Ras and ER signaling, and co-targeting may treat neurofibromin-deficient ER+ breast tumors.

2020-02-14 | GSE142479 | GEO

Neurofibromin Is an Estrogen Receptor-? Transcriptional Co-repressor in Breast Cancer.

Project description: Not available

| S-EPMC7286719 | biostudies-literature

Nuclear Estrogen Receptor alpha (ERα) interactome following estrogen and antiestrogen treatment.

Project description:The Estrogen Receptor alpha (ERα) controls key cellular functions in hormone responsive breast cancer by assembling in large functional multiprotein complexes. ERα ligands are classified as agonists and antagonist, according to the response they elicit, thus the molecular characterization of the of ERα nuclear iteractome composition following estrogen and antiestrogen stimulation whose is needed to understand their effects on estrogen target tissues, in particular breast cancer. To this aim interaction proteomics coupled to mass spectrometry (MS) was applied to map the ERα nuclear interacting partners in MCF7 breast cancer cell nuclei following estrogen and antiestrogen stimuli.

2020-09-02 | PXD018709 | Pride

Cooperative interaction between retinoic acid receptor-alpha and estrogen receptor in breast cancer.

Project description:Retinoic acid receptor-alpha (RAR alpha) is a known estrogen target gene in breast cancer cells. The consequence of RAR alpha induction by estrogen was previously unknown. We now show that RAR alpha is required for efficient estrogen receptor-alpha (ER)-mediated transcription and cell proliferation. RAR alpha can interact with ER-binding sites, but this occurs in an ER-dependent manner, providing a novel role for RAR alpha that is independent of its classic role. We show, on a genome-wide scale, that RAR alpha and ER can co-occupy regulatory regions together within the chromatin. This transcriptionally active co-occupancy and dependency occurs when exposed to the predominant breast cancer hormone, estrogen--an interaction that is promoted by the estrogen-ER induction of RAR alpha. These findings implicate RAR alpha as an essential component of the ER complex, potentially by maintaining ER-cofactor interactions, and suggest that different nuclear receptors can cooperate for effective transcriptional activity in breast cancer cells. RAR alpha silenced breast cancer MCF-7 cell lines or control siRNA in the presence of estrogen or a vehicle. MCF-7 cells were hormone-depleted for 3 d and treated with 100 nM estrogen for 12 h. There were three biological replicates for each of the four different groups.

2010-06-16 | E-GEOD-22213 | biostudies-arrayexpress

Cooperative interaction between retinoic acid receptor-alpha and estrogen receptor in breast cancer.

2010-06-09 | GSE22213 | GEO

Mass spectrometry analysis of estrogen receptor α -interacting proteins.

Project description:Quantitative mass spectrometry analysis using tandem mass tags (TMT) labelling of estrogen receptor α (ERα) pull downs. Co-immunoprecipitated proteins using a anti Erα antibody were compared quantitatively with material recovered in a mock to identify ERα-interacting proteins.

2022-10-14 | PXD025018 | Pride

An Estrogen Receptor α-bound Human Chromatin Interactome

Project description:We developed Chromatin Interaction Analysis by Paired-End Tag sequencing (ChIA-PET) for de novo detection of global chromatin interactions, and comprehensively mapped the chromatin interaction network bound by estrogen receptor α (ERα) in the human genome. We performed 454 and Illumina sequencing analyses. Keywords: Epigenetics Using 454, we examined 3 libraries: IHM001 (Estrogen Receptor ChIA-PET), IHM043 (Estrogen Receptor ChIP-PET) and IHM062 (IgG ChIA-PET) Using Illumina, we examined 4 libraries: IHM001 (Estrogen Receptor ChIA-PET replicate 1, Paired End Sequencing), IHH015 (Estrogen Receptor ChIA-PET replicate 2, Paired End Sequencing), H3K4me3 ChIP-Seq and RNA polymerase II ChIP-Seq

2009-09-11 | E-GEOD-18046 | biostudies-arrayexpress

Estrogen receptor alpha targeting in liver cancer and breast cancer

Project description:This study is to identify estrogen receptor alpha targeting in liver cancer and breast cancer using RNA-Seq and ChIP-Seq and reveal the mechanisms underlying estrogen receptor alpha in the regulation of liver cancer and breast cancer.

2023-04-06 | GSE215384 | GEO

Regulatory Sharing Between Estrogen Receptor α Bound Enhancers

Project description:Regulatory Sharing Between Estrogen Receptor α Bound Enhancers

| PRJNA613099 | ENA

Genome-wide Estrogen Receptor-alpha activation time-course

Project description:Genome-wide Estrogen Receptor-alpha activation time-course

| PRJNA487952 | ENA