Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The histone variant macroH2A1 regulates key genes for myogenic cell fusion in a splice-isoform dependent manner

ABSTRACT: The histone variant macroH2A1 regulates key genes for myogenic cell fusion in a splice-isoform dependent manner

PROVIDER: PRJNA622946 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR11430100.fastq.gz	Fastqsanger.gz
	SRR11430101.fastq.gz	Fastqsanger.gz
	SRR11430102.fastq.gz	Fastqsanger.gz
	SRR11430103.fastq.gz	Fastqsanger.gz
	SRR11430104.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 11

Similar Datasets

The histone variant macroH2A1 regulates key genes for myogenic cell fusion in a splice-isoform dependent manner [ChIP-Seq]

Project description:MacroH2A histone variants have functions in differentiation, somatic cell reprogramming and cancer. However, at the present it is not clear how macroH2As affect gene regulation to exert these functions. Here, we have addressed the question of whether the two splice isoforms of macroH2A1 differentially regulate genes in a physiological context. We have focused on myotube formation that is a key process in embryonic myogenesis and highly relevant for muscle regeneration after acute or chronic injury. We have parted from the initial observation that loss of total macroH2A1 led to a change in the morphology of myotubes differentiated ex vivo that was indicative of reduced fusion. Individual perturbation of the two isoforms in myotubes forming in vitro from myogenic C2C12 cells showed an opposing phenotype with macroH2A1.1 enhancing and macroH2A1.2 reducing fusion. Transcriptomic analysis allowed us to associate this phenotype with the differential regulation of a subset of fusion-related genes encoding components of the extracellular matrix and cell surface receptors for adhesion. In conclusion, we describe for the first time splice isoform-specific phenotypes for the histone variant macroH2A1 in a physiologic process and provide evidence for a novel, yet unknown underlying molecular mechanism of gene regulation independent of PARP1.

2020-04-03 | GSE148044 | GEO

The histone variant macroH2A1 regulates key genes for myogenic cell fusion in a splice-isoform dependent manner [RNA-Seq]

2020-04-03 | GSE147590 | GEO

The histone variant macroH2A1 regulates key genes for myogenic cell fusion in a splice-isoform dependent manner [ChIP-Seq]

Project description:The histone variant macroH2A1 regulates key genes for myogenic cell fusion in a splice-isoform dependent manner [ChIP-Seq]

| PRJNA622955 | ENA

The histone variant macroH2A1 regulates key genes for myogenic cell fusion in a splice-isoform dependent manner [RNA-Seq]

Project description:The histone variant macroH2A1 regulates key genes for myogenic cell fusion in a splice-isoform dependent manner [RNA-Seq]

| PRJNA615657 | ENA

The Histone Variant MacroH2A1 Regulates Key Genes for Myogenic Cell Fusion in a Splice-Isoform Dependent Manner.

Project description:MacroH2A histone variants have functions in differentiation, somatic cell reprogramming and cancer. However, at present, it is not clear how macroH2As affect gene regulation to exert these functions. We have parted from the initial observation that loss of total macroH2A1 led to a change in the morphology of murine myotubes differentiated ex vivo. The fusion of myoblasts to myotubes is a key process in embryonic myogenesis and highly relevant for muscle regeneration after acute or chronic injury. We have focused on this physiological process, to investigate the functions of the two splice isoforms of macroH2A1. Individual perturbation of the two isoforms in myotubes forming in vitro from myogenic C2C12 cells showed an opposing phenotype, with macroH2A1.1 enhancing, and macroH2A1.2 reducing, fusion. Differential regulation of a subset of fusion-related genes encoding components of the extracellular matrix and cell surface receptors for adhesion correlated with these phenotypes. We describe, for the first time, splice isoform-specific phenotypes for the histone variant macroH2A1 in a physiologic process and provide evidence for a novel underlying molecular mechanism of gene regulation.

| S-EPMC7290658 | biostudies-literature

The histone variant macroH2A1 regulates key genes for myogenic cell fusion in a splice-isoform dependent manner

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

2020-04-03 | GSE148045 | GEO

Epigenetic regulation of DNA repair pathway choice by macroH2A1 splice variants ensures genome stability

Project description:Epigenetic regulation of DNA repair pathway choice by macroH2A1 splice variants ensures genome stability

2020-06-03 | MSV000085541 | MassIVE

MacroH2A1 ChIP-seq from IMR90 human primary lung fibroblasts

Project description:The histone variant macroH2A1 and the poly(ADP-ribose) polymerase PARP-1 both regulate gene transcription by modulating chromatin structure and function. Of the two macroH2A1 splice variants, macroH2A1.1 and macroH2A1.2, the former is often suppressed in cancer and has the unique ability to interact with poly(ADP-ribose). Using ChIP-seq in primary lung fibroblasts, we demonstrate that macroH2A1 is incorporated into either of two spatially and functionally distinct types of chromatin; the first is marked by H3 K27 trimethylation, while the second contains a set of nine histone acetylations. MacroH2A1-regulated genes are involved in cancer progression are specifically found in macroH2A1-containing acetylated chromatin. Through the recruitment of PARP-1, macroH2A1.1 promotes the acetylation of H2B K12 and K120 which plays a key role in the regulation of macroH2A1 target genes in primary cells. The macroH2A1/PARP-1 pathway regulating H2B K12 and K120 acetylation is disrupted in cancer cells, in part, explaining macroH2A1M-bM-^@M-^Ys role in cancer suppression. Two biological replicates of the macroH2A1 ChIP and two corresponding input samples were sequenced

2014-09-15 | E-GEOD-54845 | biostudies-arrayexpress

MacroH2A1 ChIP-seq from IMR90 human primary lung fibroblasts

2014-09-15 | GSE54845 | GEO

A conserved germline-specific Dsn1 alternative splice isoform supports oocyte and embryo development

Project description:Alternative RNA splicing can generate distinct protein isoforms to allow for the differential control of cell processes across cell types. The chromosome segregation and cell division programs associated with somatic mitosis and germline meiosis display dramatic differences such as kinetochore orientation, cohesin removal, or the presence of a gap phase. These changes in chromosome segregation require alterations to the established cell division machinery. However, it remains unclear what aspects of kinetochore function and its regulatory control differ between the mitotic and meiotic cell divisions to rewire these core processes. Additionally, the alternative splice isoforms that differentially modulate distinct cell division programs have remained elusive. Here, we demonstrate that mammalian germ cells express an alternative mRNA splice isoform for the kinetochore component, DSN1, a subunit of the MIS12 complex that links the centromeres to spindle microtubules during chromosome segregation. This germline DSN1 isoform bypasses the requirement for Aurora kinase phosphorylation for its centromere localization due to the absence of a key regulatory region allowing DSN1 to display persistent centromere localization. Expression of the germline DSN1 isoform in somatic cells results in constitutive kinetochore localization, chromosome segregation errors, and growth defects, providing an explanation for its tight cell type-specific expression. Reciprocally, precisely eliminating expression of the germline-specific DSN1 splice isoform in mouse models disrupts oocyte maturation and early embryonic divisions coupled with a reduction in fertility. Together, this work identifies a germline-specific splice isoform for a chromosome segregation component and implicates its role in mammalian fertility.

2024-08-28 | PXD054119 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data