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Acetyl-lysine Reader CECR2 Drives Breast Cancer Metastasis by Coordinating Macrophage Polarization and Immune Suppression [cell line]

ABSTRACT: Acetyl-lysine Reader CECR2 Drives Breast Cancer Metastasis by Coordinating Macrophage Polarization and Immune Suppression [cell line]

PROVIDER: PRJNA622775 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11471357.fastq.gz	Fastqsanger.gz
	SRR11471358.fastq.gz	Fastqsanger.gz
	SRR11471359.fastq.gz	Fastqsanger.gz
	SRR11471360.fastq.gz	Fastqsanger.gz
	SRR11471361.fastq.gz	Fastqsanger.gz

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Similar Datasets

Acetyl-lysine Reader CECR2 Drives Breast Cancer Metastasis by Coordinating Macrophage Polarization and Immune Suppression

Project description:Acetyl-lysine Reader CECR2 Drives Breast Cancer Metastasis by Coordinating Macrophage Polarization and Immune Suppression

| PRJNA622795 | ENA

Acetyl-lysine Reader CECR2 Drives Breast Cancer Metastasis by Coordinating Macrophage Polarization and Immune Suppression [metastasis]

Project description:Acetyl-lysine Reader CECR2 Drives Breast Cancer Metastasis by Coordinating Macrophage Polarization and Immune Suppression [metastasis]

| PRJNA622783 | ENA

Acetyl-lysine Reader CECR2 Drives Breast Cancer Metastasis by Coordinating Macrophage Polarization and Immune Suppression [metastasis]

Project description:Purpose: Advanced breast cancer leads to significantly higher mortality due to metastasis. The goal of this work is to screen and study the deregulated epigenetic regulators to identify the novel targets for the treatment of metastatic breast cancer. Methods:RNA-Seq analysis of matched primary and metastatic breast samples to detect the deregulated epigenetic regulators. Live imaging system was applied to modulate metastatic tumor growth in vivo. Results: we identified that deregulated CECR2 was associated with breast cancer metastasis by RNA sequencing analysis of the matched primary and metastatic breast cancer samples from 13 patients. CECR2 knockout significantly decreased breast cancer metastasis in both immunocompromised and immunocompetent mice models. RNA-seq analysis showed that gene set "response to NF-κB signaling" was significantly decreased by CECR2 depletion in breast cancer cells. Mechanistically, CECR2 formed a complex with RELA on NF-κB target gene promoters to activate target gene expression. Furthermore, CECR2 played a key role in tumor associated macrophage recruitment and polarization, which regulates the antitumor immunity in microenvironment. Conclusions: our work identified and characterized a novel epigenetic regulator CECR2 in regulating breast cancer metastasis, and can serve as a potential target for the treatment of metastatic breast cancer.

2021-12-31 | GSE147995 | GEO

Acetyl-lysine Reader CECR2 Drives Breast Cancer Metastasis by Coordinating Macrophage Polarization and Immune Suppression [cell line]

2021-12-31 | GSE147993 | GEO

Acetyl-lysine Reader CECR2 Drives Breast Cancer Metastasis by Coordinating Macrophage Polarization and Immune Suppression

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

2021-12-31 | GSE148005 | GEO

CECR2 Drives Breast Cancer Metastasis by Suppressing Macrophage Inflammatory Responses

Project description:Purpose: Metastasis are responsible for the most majority of cancer-related deaths due to the lack of effective targeted therapies. Therefore, specific targets which tackle that complex process are needed to improve the therapeutic outcomes of metastatic breast cancer. Methods: ATAC-Seq analysis of CECR2 knockout and control LM2 cells. Results: CECR2 knockout regulate chromatin accessibility of NF-kB target genes . Conclusions: Our work confirmed that CECR2 knockout attenuates chromatin accessibility at promoters or enhancers of the downstream NF-kB target genes.

2022-01-21 | GSE185647 | GEO

Cecr2 promotes somatic cell reprogramming as a downstream target of SALL4 [ChIP-seq]

Project description:Sall4 is among one of the most important reprogramming factors. However, the underline molecular mechanisms for such importance remains unclear. In this report, we first described the gene expression and chromatin accessibility dynamics in OKS-Sall4 induced somatic cell reprogramming, and screened a group of downstream targets of Sall4, among which, cecr2, regulated by Sall4 directly, can significantly promote OKS induced reprogramming. Moreover, Cecr2 and Sall4 shared several downstream targets, such as Esrrb, Nanog, T etc., at transcription level when overexpress in the context of OKS induced reprogramming. We further showed that the DTT domain of cecr2 was responding to the reprogramming activity. Our findings provide a new important reprogramming factors and suggesting the cecr2-associted protein network may contributes to overcoming the epigenetic barriers in reprogramming.

2021-03-23 | GSE147680 | GEO

Cecr2 promotes somatic cell reprogramming as a downstream target of SALL4 [RNA-seq]

2021-03-23 | GSE147679 | GEO

Cecr2 promotes somatic cell reprogramming as a downstream target of SALL4 [ATAC-seq]

2021-03-23 | GSE147678 | GEO

ACP Acylation Is an Acetyl-CoADependent Modification Required for Electron Transport Chain Assembly

Project description:The electron transport chain (ETC) is an important participant in cellular energy conversion, but its biogenesis presents the cell with numerous challenges. To address these complexities, the cell utilizes ETC assembly factors, which include the LYR protein family. Each member of this family interacts with the mitochondrial acyl carrier protein (ACP), the scaffold protein upon which the mitochondrial fatty acid synthesis (mtFAS) pathway builds fatty acyl chains from acetyl-CoA. We demonstrate that the acylated form of ACP is an acetyl-CoA-dependent allosteric activator of the LYR protein family used to stimulate ETC biogenesis. By tuning ETC assembly to the abundance of acetyl-CoA, which is the major fuel of the TCA cycle and ETC, this system could provide an elegant mechanism for coordinating the assembly of ETC complexes with one another and with substrate availability.

2022-07-11 | PXD035000 | Pride

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