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BIN2 Inhibition Suppress Cancer Progression and Protect Ovarian function through Downregulating HDAC1 and RPS6 Phosphorylation Respectively [CUT&Tag]

ABSTRACT: BIN2 Inhibition Suppress Cancer Progression and Protect Ovarian function through Downregulating HDAC1 and RPS6 Phosphorylation Respectively [CUT&Tag]

PROVIDER: PRJNA1025851 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26320424_1.fastq.gz	Fastqsanger.gz
	SRR26320424_2.fastq.gz	Fastqsanger.gz
	SRR26320425_1.fastq.gz	Fastqsanger.gz
	SRR26320425_2.fastq.gz	Fastqsanger.gz
	SRR26320426_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

BIN2 Inhibition Suppress Cancer Progression and Protect Ovarian function through Downregulating HDAC1 and RPS6 Phosphorylation Respectively [RNA-Seq]

Project description:Malignant tumors, or cancers, are increasingly menacing people's life and health. For your female cancer patient, the ideal therapy should achieve dual purpose: suppress tumor progression meanwhile protect ovarian function. We previously showed that activated (phosphorylated) BIN2 in mouse ovaries regulates primordial follicle activation and oocyte quality through p-RPS6, and in this study, we found that BIN2 knockout or inhibition of BIN2 phosphorylation by BPP could suppress the genesis and progression of ovarian cancer. However, in human female ovarian cancer tissues, we didn’t see the increment of p-RPS6 although we observed a significant raise of p-BIN2. From this discrepancy between normal ovaries and ovarian cancer tissue, we guessed that p-BIN2 has other targets that are more important in ovarian cancer progression. Through mass spec identification, we found that only the constitutively active form of BIN2 (T423D & S424D) baits HDAC1, indicating that HDAC1 is a more important target of BIN2 in ovarian cancer. Next, we did saw Bin2 knockout or inhibition significantly decreased p-HDAC1 (S421) meanwhile increased H3K27ac. Moreover, chip seq showed that BIN2 inhibition significantly increased the binding of H3K27ac to multiple oncogenes. Besides, BIN2 knockout or inhibition could meanwhile protect ovarian function in mice with chemical carcinogen-induced in-situ ovarian cancers or with ovarian cancer cell transplantation. This study suggested that BIN2 inhibition could both suppress ovarian tumorigenesis and protect ovarian fertility, but through distinct mechanisms.

2024-07-01 | GSE244897 | GEO

BIN2 Inhibition Suppress Cancer Progression and Protect Ovarian function through Downregulating HDAC1 and RPS6 Phosphorylation Respectively [CUT&Tag]

2024-07-01 | GSE244896 | GEO

BIN2 Inhibition Suppress Cancer Progression and Protect Ovarian function through Downregulating HDAC1 and RPS6 Phosphorylation Respectively

Project description:BIN2 Inhibition Suppress Cancer Progression and Protect Ovarian function through Downregulating HDAC1 and RPS6 Phosphorylation Respectively

| PRJNA1025850 | ENA

BIN2 Inhibition Suppress Cancer Progression and Protect Ovarian function through Downregulating HDAC1 and RPS6 Phosphorylation Respectively [RNA-Seq]

Project description:BIN2 Inhibition Suppress Cancer Progression and Protect Ovarian function through Downregulating HDAC1 and RPS6 Phosphorylation Respectively [RNA-Seq]

| PRJNA1025852 | ENA

BIN2 Inhibition Suppress Cancer Progression and Protect Ovarian function through Downregulating HDAC1 Phosphorylation

Project description:Malignant tumors, or cancers, are increasingly menacing people's life and health. For your female cancer patient, the ideal therapy should achieve dual purpose: suppress tumor progression meanwhile protect ovarian function. We previously showed that activated (phosphorylated) BIN2 in mouse ovaries regulates primordial follicle activation and oocyte quality through p-RPS6, and in this study, we found that BIN2 knockout or inhibition of BIN2 phosphorylation by BPP could suppress the genesis and progression of ovarian cancer. However, in human female ovarian cancer tissues, we didn’t see the increment of p-RPS6 although we observed a significant raise of p-BIN2. From this discrepancy between normal ovaries and ovarian cancer tissue, we guessed that p-BIN2 has other targets that are more important in ovarian cancer progression. Through mass spec identification, we found that only the constitutively active form of BIN2 (T423D & S424D) baits HDAC1, indicating that HDAC1 is a more important target of BIN2 in ovarian cancer. Next, we did saw Bin2 knockout or inhibition significantly decreased p-HDAC1 (S421) meanwhile increased H3K27ac. Moreover, chip seq showed that BIN2 inhibition significantly increased the binding of H3K27ac to multiple tumor suppressors. Besides, BIN2 knockout or inhibition could meanwhile protect ovarian function in mice with chemical carcinogen-induced in-situ ovarian cancers or with ovarian cancer cell transplantation. This study suggested that BIN2 inhibition could both suppress ovarian tumorigenesis and protect ovarian fertility, but through distinct mechanisms.

2023-10-20 | PXD046297 |

BIN2 Inhibition Suppress Cancer Progression and Protect Ovarian function through Downregulating HDAC1 and RPS6 Phosphorylation Respectively

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

2024-07-01 | GSE244898 | GEO

Ribosomal protein S6 Rps6 heterozygous null deletion effect on footpad epidermis

Project description:Mutant and non-mutant footpad. McGowan et al. in press Keywords: Mutant vs. non-mutant The tissue (footpad epidermis) is from a conditional heterozygous null deletion of Rps6. One copy of Rps6 was deleted from keratinocytes in the skin using the K5.Cre transgene. K5Cre x Rps6^loxP

2008-06-12 | E-GEOD-11331 | biostudies-arrayexpress

Ribosomal protein S6 Rps6 heterozygous null deletion effect on footpad epidermis

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Phosphorylation of Ribosomal Protein RPS6 Integrates Light Signals and Circadian Clock Signals

Project description:The translation of mRNA into protein is tightly regulated by the light environment as well as by the circadian clock. Although changes in translational efficiency have been well documented at the level of mRNA-ribosome loading, the underlying mechanisms are unclear. The reversible phosphorylation of RIBOSOMAL PROTEIN OF THE SMALL SUBUNIT 6 (RPS6) has been known for forty years, but the biochemical significance of this event remains unclear to this day. Here, we confirm using a clock-deficient strain of Arabidopsis thaliana that RPS6 phosphorylation (RPS6-P) is controlled by the diel light-dark cycle with a peak during the day.

2018-08-16 | PXD008125 | Pride

mRNA expression data from livers of wild-type (WT) mice, mice that lack ribosomal protein S6 (Rps6) (DS6), mice that overexpress c-Myc (Myc) and livers that lack Rps6 and also overexpress c-Myc (DS6 Myc)

Project description:Targeted depletion of ribosomal protein S6 (Rps6) from hepatoblasts of the developing liver results in neonatal sub-lethal hepatic failure due to inhibition of bile duct development and widespread induction of hepatocyte death triggering regeneration. Overexpression of c-Myc is hepatoprotective in the context of Rps6-deficiency and eliminates the need for DS6 livers to regenerate by preventing hepatocyte death. Microarrays were used to identify the transcriptional program associated with loss of hepatic Rps6 and to identify mRNAs associated with c-Myc's hepatoprotective effect in DS6 livers

2023-01-04 | GSE212363 | GEO

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