Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

THE ACTIN-BINDING MOESIN PROTEIN IS REQUIRED FOR HEAT SHOCK GENE EXPRESSION IN DROSOPHILA

ABSTRACT: THE ACTIN-BINDING MOESIN PROTEIN IS REQUIRED FOR HEAT SHOCK GENE EXPRESSION IN DROSOPHILA

PROVIDER: PRJNA655559 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR12991410_1.fastq.gz	Fastqsanger.gz
	SRR12991410_2.fastq.gz	Fastqsanger.gz
	SRR12991411_1.fastq.gz	Fastqsanger.gz
	SRR12991411_2.fastq.gz	Fastqsanger.gz
	SRR12991412_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 18

Similar Datasets

THE ACTIN-BINDING MOESIN PROTEIN IS REQUIRED FOR HEAT SHOCK GENE EXPRESSION IN DROSOPHILA

Project description:The cytoskeletal actin-binding ERM (ezrin, radixin and moesin) proteins play essential role in modulating numerous signal transduction events in the cytoplasm by crosslinking actin filaments with plasma membrane proteins. The nuclear localization of ERMs has been also reported and the involvement of the single Drosophila ERM protein in nuclear mRNA export was recently described. However, because the cytoskeletal activity of ERMs is essential in the cell, and the exact mechanism of their nuclear transport is still unknown, the biological significance of the presence of ERM proteins in the nucleus has not been yet determined. Here we present the first attempt to reveal the in vivo relevance of the nuclear localization of the cytoskeletal ERM protein, Drosophila Moesin. With the help of a nuclear export signal (NES) we decreased the amount of Moesin in the nuclei of the animal. As a result, we observed various developmental defects, demonstrating for the first time the importance of ERM function in the cell nucleus. Transcriptome analysis of the mutant flies revealed, that the lack of nuclear Moe function leads to expression change of about 700 genes, among them a group of heat shock genes. This result together with additional findings demonstrates that in Drosophila, the expression of protein chaperons requires the nuclear functions of Moesin.

2020-08-06 | GSE155778 | GEO

RPRD1B is required for proper heat shock response [RNA-seq]

Project description:The Heat Shock response (HSR) is a highly conserved transcriptional program induced by the exposure to a variety of environmental stressors. Following an insult, a small subset of genes, known as the Heat Shock genes, are rapidly induced by the Heat Shock Factors (HSFs) to maintain protein homeostasis and ensure cell survival. In this study, we demonstrate that the RNAPII interactor RPRD1B is required for proper transcription of heat shock induced genes and for survival to heat shock.

2022-09-08 | GSE197993 | GEO

RPRD1B is required for proper heat shock response [TTchem-seq]

2022-09-08 | GSE197992 | GEO

RPRD1B is required for proper heat shock response

Project description:RPRD1B is required for proper heat shock response

| PRJNA813306 | ENA

Whole-genome analysis of heat shock factor binding sites in Drosophila melanogaster during heat shock

Project description:Whole-genome analysis of heat shock factor binding sites in Drosophila melanogaster. Heat shock factor IP DNA or Mock IP DNA from heat shocked Kc 167 cells compared to whole cell extract on Agilent 2x244k tiling arrays.

2011-01-05 | GSE19744 | GEO

Nascent-protein ubiquitination is required for heat shock-induced gene downregulation in human cells.

Project description:Proteotoxic stress such as heat shock causes heat-shock factor (HSF)-dependent transcriptional upregulation of chaperones. Heat shock also leads to a rapid and reversible downregulation of many genes, a process we term stress-induced transcriptional attenuation (SITA). The mechanism underlying this conserved phenomenon is unknown. Here we report that enhanced recruitment of negative transcription elongation factors to gene promoters in human cell lines induces SITA. A chemical inhibitor screen showed that active translation and protein ubiquitination are required for the response. We further find that proteins translated during heat shock are subjected to ubiquitination and that p38 kinase signaling connects cytosolic translation with gene downregulation. Notably, brain samples of subjects with Huntington's disease also show transcriptional attenuation, which is recapitulated in cellular models of protein aggregation similar to heat shock. Thus our work identifies an HSF-independent mechanism that links nascent-protein ubiquitination to transcriptional downregulation during heat shock, with potential ramifications in neurodegenerative diseases.

2019-02-07 | GSE112379 | GEO

RPRD1B is required for proper heat shock response [RNA-seq]

Project description:RPRD1B is required for proper heat shock response [RNA-seq]

| PRJNA813310 | ENA

RPRD1B is required for proper heat shock response [TTchem-seq]

Project description:RPRD1B is required for proper heat shock response [TTchem-seq]

| PRJNA813305 | ENA

Genome-wide binding profile for Heat Shock Factor (HSF).

Project description:Sequence-specific transcription factors (TFs) are critical for specifying patterns and levels of gene expression, but the DNA elements to which they can bind are not always sufficient to specify their binding in vivo. In eukaryotes, the binding of a TF is in competition with a constellation of other proteins, including histones which package DNA into nucleosomes. Here, we examine using the ChIP-seq assay, the genome-wide distribution of Drosophila Heat Shock Factor (HSF), a TF whose binding activity is mediated by heat shock-induced trimerization. We detect HSF binding to 464 sites, the vast majority of which contain HSF Sequence-binding Elements (HSEs) in Drosophila S2 cells, but these HSF-bound sites represent only a small fraction of HSEs present in the genome. We find a strong correlation of bound HSEs to active chromatin marks present prior to HSF binding, indicating an HSE’s residence in open chromatin is a primary determinant of whether HSF can bind following heat shock.

2010-09-02 | GSE19025 | GEO

Systemic Comparison of Heat Shock Response Induced by Heat Shock and a Proteasome Inhibitor in Mouse Fibrosarcoma Cells and Their Thermotolerant Counterparts

Project description:Heat shock response (HSR) is a cellular defense mechanism against various stresses. Both heat shock and proteasome inhibitor MG132 cause the induction of heat shock proteins, a distinct feature of HSR. To better understand the molecular basis of HSR, we subjected the mouse fibrosarcoma cell line, RIF-1, and its thermotolerant variant, TR-RIF-1 cells, to heat shock and MG132. We compared mRNA expressions using microarray analysis during recovery after heat shock and MG132 treatment. This study led us to group the 3,245 up-regulated genes by heat shock and MG132 into three families: genes regulated 1) by both heat shock and MG132 (e.g. chaperones); 2) by heat shock (e.g. DNA-binding proteins including histones); and 3) by MG132 (e.g. innate immunity and defense-related molecules).

2011-11-09 | GSE24197 | GEO

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