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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

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

PROVIDER: PRJNA422207 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR6371240.fastq.gz	Fastqsanger.gz
	SRR6371241.fastq.gz	Fastqsanger.gz
	SRR6371242.fastq.gz	Fastqsanger.gz
	SRR6371237.fastq.gz	Fastqsanger.gz
	SRR6371238.fastq.gz	Fastqsanger.gz

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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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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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Regulation of organismal proteostasis by transcellular chaperone signaling.

Project description:A major challenge for metazoans is to ensure that different tissues, each expressing distinctive proteomes, are nevertheless well protected at an organismal level from proteotoxic stress. We show that expression of endogenous metastable proteins in muscle cells, which rely on chaperones for proper folding, induces a systemic stress response throughout multiple tissues of C. elegans. Suppression of misfolding in muscle cells can be achieved not only by enhanced expression of HSP90 in muscle cells but as effectively by elevated expression of HSP90 in intestine or neuronal cells. This cell-nonautonomous control of HSP90 expression relies upon transcriptional feedback between somatic tissues that is regulated by the FoxA transcription factor PHA-4. This transcellular chaperone signaling response maintains organismal proteostasis when challenged by a local tissue imbalance in folding and provides the basis for organismal stress-sensing surveillance.

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A PQM-1-Mediated Response Triggers Transcellular Chaperone Signaling and Regulates Organismal Proteostasis.

Project description:In metazoans, tissues experiencing proteotoxic stress induce "transcellular chaperone signaling" (TCS) that activates molecular chaperones, such as hsp-90, in distal tissues. How this form of inter-tissue communication is mediated to upregulate systemic chaperone expression and whether it can be utilized to protect against protein misfolding diseases remain open questions. Using C. elegans, we identified key components of a systemic stress signaling pathway that links the innate immune response with proteostasis maintenance. We show that mild perturbation of proteostasis in the neurons or the intestine activates TCS via the GATA zinc-finger transcription factor PQM-1. PQM-1 coordinates neuron-activated TCS via the innate immunity-associated transmembrane protein CLEC-41, whereas intestine-activated TCS depends on the aspartic protease ASP-12. Both TCS pathways can induce hsp-90 in muscle cells and facilitate amelioration of Aβ3-42-associated toxicity. This may have powerful implications for the treatment of diseases related to proteostasis dysfunction.

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Dedicated chaperone at the ribosome safeguards the proteostasis network during eEF1A biogenesis

Project description:Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. Here we find that the universal cotranslational machinery adapts to accommodate the challenging biogenesis of abundantly expressed eukaryotic translation elongation factor 1A (eEF1A). During eEF1A synthesis, chaperone Chp1 is recruited to the ribosome with the help of the nascent polypeptide-associated complex (NAC), where it safeguards eEF1A biogenesis. Aberrant eEF1A production triggers instant proteolysis, widespread protein aggregation, activation of Hsf1 stress transcription and compromises cellular fitness. The expression of pathogenic eEF1A2 variants linked to epileptic-dyskinetic encephalopathy is protected by Chp1. Thus, eEF1A is a difficult to fold protein that necessitates dedicated folding factor Chp1 at the ribosomal tunnel exit to protect the eukaryotic cell from proteostasis collapse.

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