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

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

PROVIDER: PRJNA810176 | 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

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

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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]

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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.

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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.

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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.

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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.

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A microsporidia possesses robust transcriptional response to heat shock impacting diverse cellular processes despite lack of HSF

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