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PRMT1-dependent histone arginine methylation regulates mature beta cell identity

ABSTRACT: PRMT1-dependent histone arginine methylation regulates mature beta cell identity

PROVIDER: PRJNA481040 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR7521390_1.fastq.gz	Fastqsanger.gz
	SRR7521390_2.fastq.gz	Fastqsanger.gz
	SRR7521400_1.fastq.gz	Fastqsanger.gz
	SRR7521400_2.fastq.gz	Fastqsanger.gz
	SRR7521410_1.fastq.gz	Fastqsanger.gz

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PRMT1-dependent histone arginine methylation regulates mature beta cell identity (RNA-Seq)

Project description:PRMT1-dependent histone arginine methylation regulates mature beta cell identity (RNA-Seq)

| PRJNA481043 | ENA

PRMT1-dependent histone arginine methylation regulates mature beta cell identity (ChIP-Seq)

Project description:PRMT1-dependent histone arginine methylation regulates mature beta cell identity (ChIP-Seq)

| PRJNA481044 | ENA

PRMT1-dependent histone arginine methylation regulates mature beta cell identity (ATAC-Seq)

Project description:PRMT1-dependent histone arginine methylation regulates mature beta cell identity (ATAC-Seq)

| PRJNA481045 | ENA

PRMT1-dependent histone arginine methylation regulates mature beta cell identity (ATAC-Seq)

Project description:Purpose: Loss of functional β cell mass is an essential feature of type 2 diabetes and recent studies indicate that cell dedifferentiation can result in the loss of functional cell mass. However, the mechanism of cell dedifferentiation has not been elucidated due to the lack of appropriate animal model. Methods: Prmt1 floxed mice were crossed with Rip2-Cre and Pdx1-CreERT2 mice to generate Prmt1 KO and Prmt1 iKO mice. R26-eYFP mice were crossed for lineage tracing experiments and cell sorting. All mice were backcrossed and maintained on a C57BL/6J background. Cre recombination for CreERT2 was induced by total 5 times intraperitoneal injections (75 mg/kg) of corn oil dissolved tamoxifen (T5648, Sigma-Aldrich) over 2 weeks. Results: Deletion of Prmt1 in mature cells resulted in the immediate loss of H4R3me2a which induced cell dedifferentiation and cell selective Prmt1 knock-out mice developed diabetes phenotype. H4R3me2a worked as an active histone code that increased chromatin accessibility at the binding sites for transcription factors including CTCF, NKX6.1, MAFA, PDX1 and NEUROD1. Conclusions: PRMT1-dependent open chromatin regions showed a strong association with the risk of diabetes in human. In conclusion, PRMT1 plays an essential role in maintaining β cell identity by regulating chromatin accessibility.

2020-12-03 | GSE117099 | GEO

PRMT1-dependent histone arginine methylation regulates mature beta cell identity (ChIP-Seq)

2020-12-03 | GSE117097 | GEO

PRMT1-dependent histone arginine methylation regulates mature beta cell identity (RNA-Seq)

2020-12-03 | GSE117096 | GEO

PRMT1-dependent histone arginine methylation regulates mature beta cell identity

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

2020-12-03 | GSE117100 | GEO

Transcription profiling of human HeLa cells follwing siRNA mediated knock down of the arginine methyltransferases CARM1 and/or PRMT1

Project description:siRNA mediated knockdown of the arginine methyltransferases CARM1 and/or PRMT1 in HeLa cells

2007-08-30 | E-MEXP-1173 | biostudies-arrayexpress

PRMT1-dependent Arginine methylation regulates replication stress response through DNA-protein kinase

Project description:PRMT1 is the major Arginine methyltransferase in mammalian cells and its over-expression in human cancer has been linked to poor response to cancer therapy. Here, combining mass spectrometry-based global methyl-proteomics with genome-wide mRNA expression profiling, we identify PRMT1 and its associated Arginine methylation as a regulatory hubs controlling cancer cell response to replicative stress agents. We show that DNA-PK binds to PRMT1 and regulates both its subcellular localization and activity, leading to PRMT1 recruitment to drug-stalled replication forks and channelling its methyl-transferase activity from its soluble targets towards Arginine 3 of histone H4. This DNA-PK-PRMT1 axis is required for the induction of the Senescence-Associated Secretory Phenotype, which sustains cell cycle arrest and protects cells from apoptosis. Our data show that Arginine-methylation regulates the adaptive response of cancer cell to replicative stress agents and might be targeted to sensitize cancer cells to genotoxic chemotherapeutics

2020-01-14 | GSE106609 | GEO

The arginine methyltransferase PRMT1 establishes transcriptomic homeostasis essential for spermatogonial differentiation and male fertility

Project description:Protein arginine methyltransferase 1 (Prmt1) is known as the major Type-I protein arginine methyltransferase that deposits asymmetrical dimethylarginine (ADMA) in both histone and non-histone substrates. Nonetheless, how Prmt1 and its downstream signalling through substrate methylation function in the male germline development remains poorly understood. In this study, we discovered that Prmt1 is predominantly present in the spermatogonial population during mouse spermatogenesis. Using three Cre-mediated conditional Prmt1 knockout mouse lines, we observed that Prmt1 is essential for the maintenance of spermatogonial cells and Prmt1-deposited ADMA marks coordinate an inherent homeostasis among three types of substrate methylation. In conjunction with high-throughput Cut&Tag and modified mini-bulk Smart-seq2 analyses, we unveiled that Prmt1-mediated H4R3me2a mark enriched in the promoter region, together with other histone arginine methylations, drives a global transcriptomic landscape that maintains the regular gene expression and alternative splicing. Collectively, we provide the genetic evidence showing the essential role of Prmt1-deposited arginine methylation in the establishment of transcriptional homeostasis, and shed light on the methylarginine signalling pathway in orchestrating spermatogonial development in the mammalian germline.

2023-03-31 | GSE227857 | GEO

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