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Hsf1 promotes hematopoietic stem cell fitness and proteostasis in response to ex vivo culture stress and aging II

ABSTRACT: Hsf1 promotes hematopoietic stem cell fitness and proteostasis in response to ex vivo culture stress and aging II

PROVIDER: PRJNA743655 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15037700_1.fastq.gz	Fastqsanger.gz
	SRR15037700_2.fastq.gz	Fastqsanger.gz
	SRR15037701_1.fastq.gz	Fastqsanger.gz
	SRR15037701_2.fastq.gz	Fastqsanger.gz
	SRR15037702_1.fastq.gz	Fastqsanger.gz

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Hsf1 promotes hematopoietic stem cell fitness and proteostasis in response to ex vivo culture stress and aging II

Project description:Maintaining proteostasis is key to resisting stress and to promoting healthy aging. Proteostasis is necessary to preserve stem cell function, but little is known about the mechanisms that regulate proteostasis during stress in stem cells, and whether disruptions in proteostasis contribute stem cell aging is largely unexplored. We determined that ex vivo cultured mouse and human hematopoietic stem cells (HSCs) rapidly increase protein synthesis. This challenge to HSC proteostasis was associated with nuclear accumulation of Hsf1, and deletion of Hsf1 impaired HSC maintenance ex vivo. Strikingly, supplementing cultures with small molecules that enhance Hsf1 activation partially suppressed protein synthesis, rebalanced proteostasis, and supported retention of HSC serial reconstituting activity. Although Hsf1 was dispensable for young adult HSCs in vivo, Hsf1 deficiency increased protein synthesis and impaired the reconstituting activity of middle-aged HSCs. Hsf1 thus promotes proteostasis and the regenerative activity of HSCs in response to culture stress and aging.

2021-07-11 | GSE179413 | GEO

Hsf1 promotes hematopoietic stem cell fitness and proteostasis in response to ex vivo culture stress and aging I

2021-07-11 | GSE179412 | GEO

Hsf1 promotes hematopoietic stem cell fitness and proteostasis in response to ex vivo culture stress and aging

Project description:Hsf1 promotes hematopoietic stem cell fitness and proteostasis in response to ex vivo culture stress and aging

| PRJNA743654 | ENA

Hsf1 promotes hematopoietic stem cell fitness and proteostasis in response to ex vivo culture stress and aging I

Project description:Hsf1 promotes hematopoietic stem cell fitness and proteostasis in response to ex vivo culture stress and aging I

| PRJNA743652 | ENA

Hsf1 promotes hematopoietic stem cell fitness and proteostasis in response to ex vivo culture stress and aging.

Project description:Maintaining proteostasis is key to resisting stress and promoting healthy aging. Proteostasis is necessary to preserve stem cell function, but little is known about the mechanisms that regulate proteostasis during stress in stem cells, and whether disruptions of proteostasis contribute to stem cell aging is largely unexplored. We determined that ex-vivo-cultured mouse and human hematopoietic stem cells (HSCs) rapidly increase protein synthesis. This challenge to HSC proteostasis was associated with nuclear accumulation of Hsf1, and deletion of Hsf1 impaired HSC maintenance ex vivo. Strikingly, supplementing cultures with small molecules that enhance Hsf1 activation partially suppressed protein synthesis, rebalanced proteostasis, and supported retention of HSC serial reconstituting activity. Although Hsf1 was dispensable for young adult HSCs in vivo, Hsf1 deficiency increased protein synthesis and impaired the reconstituting activity of middle-aged HSCs. Hsf1 thus promotes proteostasis and the regenerative activity of HSCs in response to culture stress and aging.

| S-EPMC8571035 | biostudies-literature

Hsf1 promotes hematopoietic stem cell fitness and proteostasis in response to ex vivo culture stress and aging

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

2021-07-11 | GSE179415 | GEO

HSF1 Activation Can Restrict HIV Replication

Project description:Host protein folding stress responses can play important roles in RNA virus replication and evolution. Intriguingly, prior work revealed a complicated interplay between the cytosolic proteostasis stress response, controlled by its master regulator heat shock factor 1 (HSF1) and human immunodeficiency virus-1 (HIV-1). We sought to isolate HSF1 transcription factor activity from proteostasis stress and elucidate the function of HSF1 in HIV-1 lifecycle in absence of cellular stress. We used chemical genetic, stress-independent control of HSF1 activity to establish whether and how HSF1 influences HIV-1 replication. Stress-independent HSF1 induction decreased both the total quantity and infectivity of HIV-1 virions. Moreover, HIV-1 was unable to escape HSF1-mediated restriction over the course of several serial passages. These results promote continued consideration of the heat shock response as a potential target for antiviral drugs.

2022-01-30 | GSE137591 | GEO

An HSF1-JMJD6-HSP feedback circuit promotes cell adaptation to proteotoxic stress [RNA-Seq]

Project description:Heat Shock Factor 1 (HSF1) is best known as the master transcriptional regulator of the heat-shock response (HSR), a conserved adaptive mechanism critical for protein homeostasis (proteostasis). Combining a genome-wide RNAi library with an HSR reporter, we identified JMJD6 as an essential mediator of HSF1 activity. In follow-up studies, we found that JMJD6 is itself a non-canonical transcriptional target of HSF1 which acts as a critical regulator of proteostasis. In a positive feedback circuit, HSF1 binds and promotes JMJD6 expression, which in turn reduces HSP70 R469 monomethylation to disrupt HSP70-HSF1 repressive complexes resulting in enhanced HSF1 activation. Thus, JMJD6 is intricately wired into the proteostasis network where it plays a critical role for cellular adaptation to proteotoxic stress.

2024-07-18 | GSE270672 | GEO

An HSF1-JMJD6-HSP feedback circuit promotes cell adaptation to proteotoxic stress [ChIP-Seq]

2024-07-18 | GSE270671 | GEO

Regulation of the Hsf1-dependent transcriptome via conserved bipartite contacts with Hsp70 promotes survival in yeast

Project description:Protein homeostasis and cellular fitness in the presence of proteotoxic stress is promoted by heat shock factor 1 (HSF1), which controls basal and stress-induced expression of molecular chaperones and other targets. The major heat shock proteins Hsp70 and Hsp90 in turn participate in a negative feedback loop that ensures appropriate coordination of the heat shock response with environmental conditions. Features of this regulatory circuit in the budding yeast Saccharomyces cerevisiae have been recently defined, most notably regarding direct interaction between Hsf1 and the constitutively expressed Hsp70 Ssa1. We sought to further explore the complex nature of Ssa1/Hsf1 regulation. Ssa1 is found to interact independently with both the previously defined CE2 site in the Hsf1 carboxyl-terminal transcriptional activation domain as well as a novel site that we identify within the amino-terminal activation domain. Consistent with both sites bearing a recognition signature for Hsp70, we demonstrate that Ssa1 contacts Hsf1 using its substrate binding domain and abolishing either regulatory site results in loss of Ssa1 association. Removing Hsp70 regulation of Hsf1 results in global dysregulation of Hsf1 transcriptional activity, with synergistic effects when both sites are disrupted together on both gene expression and cellular fitness. Finally, we find that Hsp70 interacts with both transcriptional activation domains of Hsf1 in the related yeast Lachancea kluyveri, implying a conserved mechanism of regulation to promote cellular proteostasis.

2019-04-16 | GSE129832 | GEO

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