Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Protein arginine methyltransferase 5 mediates the increase in interferon stimulated genes during replication stress

ABSTRACT: Protein arginine methyltransferase 5 mediates the increase in interferon stimulated genes during replication stress

PROVIDER: PRJNA993140 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR25222023_1.fastq.gz	Fastqsanger.gz
	SRR25222023_2.fastq.gz	Fastqsanger.gz
	SRR25222024_1.fastq.gz	Fastqsanger.gz
	SRR25222024_2.fastq.gz	Fastqsanger.gz
	SRR25222025_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 32

Similar Datasets

Protein arginine methyltransferase 5 mediates the increase in interferon stimulated genes during replication stress

Project description:Replication stress (RS) is a hallmark of cancer and is defined as the perturbation of DNA replication that results in stalled or collapsed DNA replication forks. Chemotherapeutic drugs exploit this phenomenon by enhancing the RS, resulting in cell death. Protein arginine methyltransferase 5 (PRMT5) is responsible for post-translational symmetric dimethylarginine (SDMA) modification. This modification is important for regulating RS. PRMT5 is upregulated in several malignancies and therefore inhibitors have been developed. To understand the consequences of PRMT5 inhibition, we investigated its role in replication stress response. Employing the RS inducer hydroxyurea (HU) and the PRMT5 inhibitor GSK591, we discovered a PRMT5-mediated increase in SDMA during RS. Furthermore, we observed that RS resulted in a PRMT5-dependent transcriptional increase in interferon-stimulated genes (ISGs). Therefore, we demonstrated a previously unreported role for PRMT5-mediated SDMA in the context of RS.

2024-08-30 | GSE236930 | GEO

Arginine methyltransferase regulates monocyte extravasation and function

Project description:Arginine methyltransferase regulates monocyte extravasation and function

| PRJNA767361 | ENA

Protein arginine methyltransferase PRMT1 is essential for palatogenesis

Project description:Protein arginine methyltransferase PRMT1 is essential for palatogenesis

| PRJNA472987 | ENA

Epigenetic regulation of cardiac maturation by arginine methyltransferase Carm1

Project description:Epigenetic regulation of cardiac maturation by arginine methyltransferase Carm1

| PRJNA809345 | ENA

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

Protein Arginine Methyltransferase 1 is therapeutic vulnerability in Multiple Myeloma

Project description:Protein Arginine Methyltransferase 1 is therapeutic vulnerability in Multiple Myeloma

| PRJNA983271 | ENA

Histone arginine methyltransferase CARM1 Is Crucial for Epigenetic Regulation of Starvation-induced Autophagy

Project description:Autophagy is a highly conserved self-digestion process, essential to maintain homeostasis and viability in response to nutrient starvation. Although the components of autophagy in the cytoplasm have been well-studied, molecular basis for the epigenetic regulation of autophagy is poorly understood. Here, we identify histone arginine methyltransferase CARM1 as a critical component of autophagy. We found that nutrient starvation increased CARM1 protein level and subsequently histone H3R17 dimethylation. Genome-wide analyses reveal that CARM1 exerts transcriptional coactivator function on autophagy-related genes and lysosomal genes through TFEB. Our findings demonstrate a previously unrecognized role of CARM1-dependent histone arginine methylation as a critical nuclear event of autophagy.

2016-06-17 | GSE72901 | GEO

Epigenetic regulation of cardiac maturation by arginine methyltransferase Carm1 (ATAC-Seq)

Project description:Epigenetic regulation of cardiac maturation by arginine methyltransferase Carm1 (ATAC-Seq)

| PRJNA809351 | ENA

Epigenetic regulation of cardiac maturation by arginine methyltransferase Carm1 (RNA-Seq)

Project description:Epigenetic regulation of cardiac maturation by arginine methyltransferase Carm1 (RNA-Seq)

| PRJNA809349 | ENA

Epigenetic regulation of cardiac maturation by arginine methyltransferase Carm1 (ChIP-Seq)

Project description:Epigenetic regulation of cardiac maturation by arginine methyltransferase Carm1 (ChIP-Seq)

| PRJNA809350 | ENA