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Transcellular chaperone signaling is an intercellular stress-response that is distinct from the HSF-1 mediated HSR

ABSTRACT: Transcellular chaperone signaling is an intercellular stress-response that is distinct from the HSF-1 mediated HSR

PROVIDER: PRJNA810171 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18134207_1.fastq.gz	Fastqsanger.gz
	SRR18134207_2.fastq.gz	Fastqsanger.gz
	SRR18134208_1.fastq.gz	Fastqsanger.gz
	SRR18134208_2.fastq.gz	Fastqsanger.gz
	SRR18134209_1.fastq.gz	Fastqsanger.gz

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Transcellular chaperone signaling is an intercellular stress-response that is distinct from the HSF-1 mediated HSR [WGS]

Project description:Transcellular chaperone signaling is an intercellular stress-response that is distinct from the HSF-1 mediated HSR [WGS]

| PRJNA810175 | ENA

Transcellular chaperone signaling is an intercellular stress-response that is distinct from the HSF-1 mediated HSR [RNA-seq]

Project description:Transcellular chaperone signaling is an intercellular stress-response that is distinct from the HSF-1 mediated HSR [RNA-seq]

| PRJNA810176 | ENA

Transcellular chaperone signaling is an intercellular stress-response that is distinct from the HSF-1 mediated HSR [RNA-seq]

Project description:The goal of this RNA-Seq analysis was to identify genes differentially expressed in a C. elegans strain expressing a neuron-specific or gut-specific hsp-90 hairpin RNAi construct compared to control animals of the same genetic background (strain AM994). Tissue-specific expression of an hsp-90 hairpin RNAi construct knocks down hsp-90 in a tissue-specific manner and induces transcellular chaperone signalling that enhances organismal proteostasis. This study aimed to identify components of the signalling pathway responsible for this effect.

2022-02-27 | GSE197410 | GEO

Transcellular chaperone signaling is an intercellular stress-response that is distinct from the HSF-1 mediated HSR

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

2022-02-27 | GSE197412 | GEO

Transcellular chaperone signaling is an intercellular stress-response that is distinct from the HSF-1 mediated HSR [WGS]

Project description:The goal of this Whole Genome Sequencing (WGS) analysis was to identify genes underlying TCS in C. elegans strain expressing the gut-specific hsp-90 hairpin RNAi construct compared to a control strain (strain AM994). To do this we performed a forward genetic screen using the mutagen EMS and screened progeny for reduced TCS-mediated expression of the hsp-70p::mCherry reporter in muscle cells.

2022-02-27 | GSE197411 | GEO

Transcellular chaperone signaling is an intercellular stress-response distinct from the HSF-1-mediated heat shock response.

Project description:Organismal proteostasis is maintained by intercellular signaling processes including cell nonautonomous stress responses such as transcellular chaperone signaling (TCS). When TCS is activated upon tissue-specific knockdown of hsp-90 in the Caenorhabditis elegans intestine, heat-inducible hsp-70 is induced in muscle cells at the permissive temperature resulting in increased heat stress resistance and lifespan extension. However, our understanding of the molecular mechanism and signaling factors mediating transcellular activation of hsp-70 expression from one tissue to another is still in its infancy. Here, we conducted a combinatorial approach using transcriptome RNA-Seq profiling and a forward genetic mutagenesis screen to elucidate how stress signaling from the intestine to the muscle is regulated. We find that the TCS-mediated "gut-to-muscle" induction of hsp-70 expression is suppressed by HSF-1 and instead relies on transcellular-X-cross-tissue (txt) genes. We identify a key role for the PDZ-domain guanylate cyclase txt-1 and the homeobox transcription factor ceh-58 as signaling hubs in the stress receiving muscle cells to initiate hsp-70 expression and facilitate TCS-mediated heat stress resistance and lifespan extension. Our results provide a new view on cell-nonautonomous regulation of "inter-tissue" stress responses in an organism that highlight a key role for the gut. Our data suggest that the HSF-1-mediated heat shock response is switched off upon TCS activation, in favor of an intercellular stress-signaling route to safeguard survival.

| S-EPMC9956597 | biostudies-literature

The zinc finger transcription factor PQM-1 is a mediator of transcellular chaperone signalling and novel regulator of proteostasis in C. elegans

Project description:The goal of this RNA-Seq analysis was to identify genes differentially expressed in a C. elegans strain overexpressing HSP-90 in the neurons compared to control (N2) animals. C. elegans overexpressing HSP-90 protein in the neurons activate transcellular chaperone signalling that enhances organismal proteostasis. This study aimed to identify components of the signalling pathway responsible for this effect.

2018-06-05 | GSE108005 | GEO

HSF-1 promotes longevity through ubiquilin-1 dependent mitochondrial remodelling

Project description:Impaired protein homeostasis promotes age-associated tissue dysregulation, presenting a need for therapeutic approaches that can restore proteome integrity. The heat shock factor HSF-1 is the master transcriptional regulator of proteostasis and regulates the expression of heat shock proteins (HSPs), which facilitate proper protein folding, localisation, and degradation. Increased HSF-1 activity can suppress proteotoxicity and enhance longevity across species. Studies into the mechanisms behind these beneficial effects have mostly focused on HSPs; however, the precise mechanisms by which increased HSF-1 activity extends lifespan are not known. To address this, we conducted an RNAi screen for genes that promote longevity, in C. elegans over expressing HSF-1 (hsf-1 OE). We found that ubiquilin-1 (ubql-1), a multifaceted shuttle protein that functions in protein degradation pathways is necessary for full lifespan extension in hsf-1OE worms. Surprisingly, we find that lack of ubql-1 does not impact proteostasis capacity, but does alter mitochondrial dynamics, in hsf-1 OE worms. These effects are independent of mitophagy or the mitochondrial unfolded protein response (mitoUPR) suggesting enhanced turnover of mitochondrial outer membrane proteins may be important for increased longevity via the HSF-1-ubiquilin-1 axis. Additionally, we reveal a role for ubql-1, a protein quality control regulator in regulating lipid homeostasis in hsf-1 OE animals. Lack of ubql-1 in hsf-1 OE animals supresses the expression of a key mitochondrial β-oxidation and lipid mobilization gene regulated by NHR-49 - acyl-CoA synthetase-2, ACS-2 amongst other genes. We propose that ubql-1 is required for mito-fusion and metabolic modulations that promote longevity in hsf-1 OE by interacting with NHR-49.

2024-10-17 | PXD044595 | Pride

Coturnix coturnix strain:HSR

Project description:Coturnix coturnix strain:HSR Genome sequencing

| PRJNA261665 | ENA

Halanaeroarchaeum sp. HSR-CO

Project description:Halanaeroarchaeum sp HSR-CO Genome sequencing

| PRJNA752267 | ENA