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Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation

ABSTRACT: Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation

PROVIDER: PRJNA1088549 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28361115.fastq.gz	Fastqsanger.gz
	SRR28361116.fastq.gz	Fastqsanger.gz
	SRR28361117.fastq.gz	Fastqsanger.gz
	SRR28361118.fastq.gz	Fastqsanger.gz
	SRR28361119.fastq.gz	Fastqsanger.gz

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Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation (RNA-Seq)

Project description:Atherosclerosis, which develops in the inner layer of arteries, is the major cause of myocardial infarction and stroke. Atherosclerotic plaques develop preferentially in arterial regions exposed to disturbed blood flow, such as vessel curvatures, bifurcations and branching points, where endothelial cells develop an inflammatory phenotype. How disturbed flow induces endothelial cell inflammation is incompletely understood. We show here that histone H3.3 phosphorylation at serine 31 (H3.3S31) plays a critical role in disturbed flow-induced endothelial inflammation, as it allows the rapid induction of FOS and FOSB, which are required for disturbed flow-induced inflammatory gene expression. We identified protein kinase N1 (PKN1) as the kinase responsible for disturbed flow-induced H3.3S31 phosphorylation. PKN1 becomes activated by disturbed flow in an integrin a5b1-dependent manner and then translocates to the cell nucleus. We found that PKN1 is also involved in the phosphorylation of the AP-1 transcription factor JUN. Mice with endothelium-specific loss of PKN1 or endothelial expression of S31 phosphorylation-deficient mutants of H.3.3 show reduced endothelial inflammation and disturbed flow-induced vascular remodeling in vitro and in vivo. Our data identify a novel mechanism of H3.3S31 phosphorylation which may serve as a target for preventive and therapeutic anti-atherosclerotic strategies.

2024-11-26 | GSE261753 | GEO

Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation (ATAC-Seq II)

2024-11-26 | GSE261755 | GEO

Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation (ATAC-Seq I)

2024-11-26 | GSE261754 | GEO

Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation (RNA-Seq)

Project description:Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation (RNA-Seq)

| PRJNA1088551 | ENA

Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation (ATAC-Seq II)

Project description:Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation (ATAC-Seq II)

| PRJNA1088552 | ENA

Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation (ATAC-Seq I)

Project description:Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation (ATAC-Seq I)

| PRJNA1088553 | ENA

H3.3 S31 phosphorylation ChIP-seq in mitotic WT mouse ES cells

Project description:The serine 31 (S31) residue of histone H3.3 is phosphorylated during mitosis and this modification is enriched at repetitive DNA. ChIP-seq of H3.3 S31Ph was carried out in a mitotic population of synchronised mouse ES cells. We find that H3.3 S31Ph is enriched at telomeres and IAP repeats in mitotic mouse ES cells.

2022-04-10 | GSE181692 | GEO

Protein kinase N1 mediates phosphorylation of H3.3 serine 31 for rapid gene activation

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

2024-11-26 | GSE261756 | GEO

Phosphorylation of histone H3.3 at serine 31 promotes p300 activity and enhancer acetylation.

Project description:The histone variant H3.3 is enriched at enhancers and active genes, as well as repeat regions such as telomeres and retroelements, in mouse embryonic stem cells (mESCs)1-3. Although recent studies demonstrate a role for H3.3 and its chaperones in establishing heterochromatin at repeat regions4-8, the function of H3.3 in transcription regulation has been less clear9-16. Here, we find that H3.3-specific phosphorylation17-19 stimulates activity of the acetyltransferase p300 in trans, suggesting that H3.3 acts as a nucleosomal cofactor for p300. Depletion of H3.3 from mESCs reduces acetylation on histone H3 at lysine 27 (H3K27ac) at enhancers. Compared with wild-type cells, those lacking H3.3 demonstrate reduced capacity to acetylate enhancers that are activated upon differentiation, along with reduced ability to reprogram cell fate. Our study demonstrates that a single amino acid in a histone variant can integrate signaling information and impact genome regulation globally, which may help to better understand how mutations in these proteins contribute to human cancers20,21.

| S-EPMC6598431 | biostudies-literature

Sexual differentiation controlled by RNA polymerase II CTD phosphorylation on serine 2

Project description:The switch from cellular proliferation to differentiation occurs to a large extend through specific programs of gene expression. In fission yeast, the high-mobility-group transcription factor Ste11 is the master regulator of sexual differentiation. ste11 is induced by environmental conditions, mostly nitrogen starvation, leading to mating and meiosis 1. We have used ChIP-chip and gene expression profiling to show that CDK-dependent phosphorylation of serine 2 in the C-terminal domain (CTD) of the largest subunit of the RNA polymerase II (PolII) holoenzyme plays a critical role in the induction of ste11 transcription during sexual differentiation while it has a minor impact on gene expression during vegetative growth. Moreover, we demonstrate that both the recruitment of the CTD serine 2 kinase and the phosphorylation event initiate at the promoter region of ste11 in contrast to the classical case where serine 2 phosphorylation occurs across the coding region 2. In the absence of CTD serine 2 phosphorylation, both PolII occupancy at the ste11 locus, and ste11 expression are impaired. This results in sterility that is rescued when ste11 is expressed from the canonical adh promoter. We conclude that a modification of the RNA polymerase II holoenzyme plays a specific and pivotal role in the sexual differentiation. For the ChIP-chip experiments, 3-4 biological replicates were performed for each tagged protein of interest. For the expression experiments, two biological samples were hybridized for each mutant strain (replicates 1 and 2), with two dye-swap technical replicates per sample (replicates 3 and 4).

2010-01-01 | E-GEOD-16498 | biostudies-arrayexpress

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