Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Arginine methyltransferase regulates monocyte extravasation and function

ABSTRACT: Arginine methyltransferase regulates monocyte extravasation and function

PROVIDER: PRJNA767361 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR16117659_1.fastq.gz	Fastqsanger.gz
	SRR16117659_2.fastq.gz	Fastqsanger.gz
	SRR16117660_1.fastq.gz	Fastqsanger.gz
	SRR16117660_2.fastq.gz	Fastqsanger.gz
	SRR16117661_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 32

Similar Datasets

Arginine methyltransferase regulates monocyte extravasation and function

Project description:Extravasation of monocytes into tissue and to the site of injury is a fundamental immunological process underlying a variety of innate inflammatory responses across multiple organ systems, which requires rapid responses via post translational modifications (PTM) of proteins. Specifically, methylation of protein by arginine methyltransferases (PRMTs) is an epigenetic PTM implicated in inflammatory responses. However, how methyltransferases drive immune regulation particularly in the lung, the resultant tissue injury and whether this might be of therapeutic value has remained unclear. Here, we demonstrate that PRMT7 was increased in the lung of chronic obstructive pulmonary disease (COPD) patients and positively correlated with tissue injury. Accordingly, in clinically relevant models of COPD, lung fibrosis and skin injury, mice with reduced expression of PRMT7 were protected against disease development, due to decreased recruitment of pro-inflammatory monocytes to the site of injury. Mechanistically, we discovered in monocytes activation of NF-κB/RelA induces PRMT7, promoting mono-methylation of histones, which crucially regulates RAP1A and subsequent adhesion and migration ability. Furthermore, in pro-inflammatory monocytes, ALOX5 derived LTB4 induced ACSL4 expression in lung epithelial cells and consequently sensitized towards ferroptosis, thus aggravating tissue injury. Conclusively, specific targeting of arginine mono-methylation offers yet-unappreciated therapeutic potential against monocyte-driven inflammatory conditions.

2021-12-16 | GSE185006 | GEO

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

Protein arginine methyltransferase 5 regulates AKT activation via methylation to promote metastasis

Project description:Protein arginine methyltransferase 5 regulates AKT activation via methylation to promote metastasis

| PRJNA739706 | ENA

Lung macrophages mediate helminth resistance through differential activation of recruited monocyte-derived alveolar macrophages and arginine depletion

Project description:Lung macrophages mediate helminth resistance through differential activation of recruited monocyte-derived alveolar macrophages and arginine depletion

2022-01-13 | GSE189674 | 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

Protein Arginine Methyltransferase 1 is therapeutic vulnerability in Multiple Myeloma

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

| PRJNA983271 | ENA

Arginine methylation regulates widespread alternative polyadenylation

Project description:Alternative polyadenylation (APA) has recently been recognized as a universal mechanism for gene regulation, but it remains unclear how APA is controlled. Here we report that the Arabidopsis thaliana Protein Arginine Methyltransferase 10 (AtPRMT10) regulates global APA with its protein partner HLP1, a conserved hnRNP A/B protein. HLP1 binds preferentially to A-rich and U-rich cis-elements around polyadenylation sites, thereby linking AtPRMT10 to the control of APA through protein-protein interactions. AtPRMT10 mutations cause significant proximal-to-distal poly(A) site shifts largely overlapping with those in hlp1-1 mutants. Proximal polyadenylation is maintained by AtPRMT10-directed methylation and is mediated in part by methylation of HLP1 at specific arginine residues. Our findings demonstrate that arginine methylation of an RNA-binding protein adds a novel layer of regulation to widespread alternative polyadenylation.

2019-01-01 | GSE69904 | GEO

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 (ChIP-Seq)

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

| PRJNA809350 | ENA