HSF-1 displays nuclear stress body formation in multiple tissues in Caenorhabditis elegans upon stress and following the transition to adulthood

Deonarine, Andrew; Walker, Matt W.G.

doi:10.1007/s12192-020-01188-9

Cited by 10 publications

(8 citation statements)

References 47 publications

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“…Gonadal stem cells are depleted in glp-1 mutant animals, which encodes the C. elegans ortholog of the NOTCH receptor, and glp-1 mutations increase lifespan dependent on hsf-1 (Hansen et al, 2005). Interestingly, shortly after the onset of reproduction the inducibility of the HRS drops dramatically (Labbadia and Morimoto 2015b), and HSF-1 forms nuclear stress bodies at the initiation of reproduction throughout the germline and upon transition to adulthood HSF-1 stress bodies form in most somatic cells (Deonarine et al, 2021). However, this repression of the HSR does not occur in glp-1 mutant animals (Shemesh et al, 2013) and genetic loss of the germline suppressed nuclear stress body formation with age (Deonarine et al, 2021), which suggests alterations in gonadal stem cell signaling cell nonautonomously reprograms somatic maintenance, at least in part through HSF-1 activity.…”

Section: Hsf-1 Integrates Metabolic Signals To Extend C Elegans Longe...mentioning

confidence: 99%

“…Interestingly, shortly after the onset of reproduction the inducibility of the HRS drops dramatically (Labbadia and Morimoto 2015b), and HSF-1 forms nuclear stress bodies at the initiation of reproduction throughout the germline and upon transition to adulthood HSF-1 stress bodies form in most somatic cells (Deonarine et al, 2021). However, this repression of the HSR does not occur in glp-1 mutant animals (Shemesh et al, 2013) and genetic loss of the germline suppressed nuclear stress body formation with age (Deonarine et al, 2021), which suggests alterations in gonadal stem cell signaling cell nonautonomously reprograms somatic maintenance, at least in part through HSF-1 activity. Interestingly, genetic perturbation of the extracellular vitelline layer of an internally fertilized embryo initiates a transcellular signal to improve proteostasis and stress resistance in an HSF-1 dependent manner (Sala et al, 2020).…”

Section: Hsf-1 Integrates Metabolic Signals To Extend C Elegans Longe...mentioning

confidence: 99%

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HSF-1: Guardian of the Proteome Through Integration of Longevity Signals to the Proteostatic Network

et al. 2022

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Discoveries made in the nematode Caenorhabditis elegans revealed that aging is under genetic control. Since these transformative initial studies, C. elegans has become a premier model system for aging research. Critically, the genes, pathways, and processes that have fundamental roles in organismal aging are deeply conserved throughout evolution. This conservation has led to a wealth of knowledge regarding both the processes that influence aging and the identification of molecular and cellular hallmarks that play a causative role in the physiological decline of organisms. One key feature of age-associated decline is the failure of mechanisms that maintain proper function of the proteome (proteostasis). Here we highlight components of the proteostatic network that act to maintain the proteome and how this network integrates into major longevity signaling pathways. We focus in depth on the heat shock transcription factor 1 (HSF1), the central regulator of gene expression for proteins that maintain the cytosolic and nuclear proteomes, and a key effector of longevity signals.

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Section: Hsf-1 Integrates Metabolic Signals To Extend C Elegans Longe...mentioning

confidence: 99%

Section: Hsf-1 Integrates Metabolic Signals To Extend C Elegans Longe...mentioning

confidence: 99%

HSF-1: Guardian of the Proteome Through Integration of Longevity Signals to the Proteostatic Network

et al. 2022

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“…nSBs require HSF-1 binding and are a sign of activation of the HSR ( Morton and Lamitina, 2013 ). After HSR activation, nSBs form within 5 min of stress detection and gradually dissolve until HSF-1 is diffuse in the nucleus ( Figure 4A ) ( Deonarine et al, 2021 ). We examined the effect of cbp-1 RNAi on the rate of nSB recovery after stress.…”

Section: Resultsmentioning

confidence: 99%

“…Upon activation of the HSR, HSF-1 undergoes localization changes and forms nuclear stress bodies (nSBs), a hallmark of HSF-1 activation ( Deonarine et al, 2021 ). nSBs require HSF-1 binding and are a sign of activation of the HSR ( Morton and Lamitina, 2013 ).…”

Section: Resultsmentioning

confidence: 99%

“…A hallmark of HSF1 activation in both mammalian cells and C. elegans is the formation and resolution of nuclear stress bodies (nSBs) containing HSF1 ( Jolly et al, 1999 ; Jolly et al, 2004 ; Biamonti and Vourc’h, 2010 ; Morton and Lamitina, 2013 ; Deonarine et al, 2021 ). In mammalian cells, the resolution of nSBs correlates with HSF1 activity, transcription of hsp target genes, and cell survival at the single cell level ( Gaglia et al, 2020 ).…”

Section: Discussionmentioning

confidence: 99%

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The CBP-1/p300 Lysine Acetyltransferase Regulates the Heat Shock Response in C. elegans

Barrett

2022

Front. Aging

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The decline of proteostasis is a hallmark of aging that is, in part, affected by the dysregulation of the heat shock response (HSR), a highly conserved cellular response to proteotoxic stress in the cell. The heat shock transcription factor HSF-1 is well-studied as a key regulator of proteostasis, but mechanisms that could be used to modulate HSF-1 function to enhance proteostasis during aging are largely unknown. In this study, we examined lysine acetyltransferase regulation of the HSR and HSF-1 in C. elegans. We performed an RNA interference screen of lysine acetyltransferases and examined mRNA expression of the heat-shock inducible gene hsp-16.2, a widely used marker for HSR activation. From this screen, we identified one acetyltransferase, CBP-1, the C. elegans homolog of mammalian CREB-binding protein CBP/p300, as a negative regulator of the HSR. We found that while knockdown of CBP-1 decreases the overall lifespan of the worm, it also enhances heat shock protein production upon heat shock and increases thermotolerance of the worm in an HSF-1 dependent manner. Similarly, we examined a hallmark of HSF-1 activation, the formation of nuclear stress bodies (nSBs). In analyzing the recovery rate of nSBs, we found that knockdown of CBP-1 enhanced the recovery and resolution of nSBs after stress. Collectively, our studies demonstrate a role of CBP-1 as a negative regulator of HSF-1 activity and its physiological effects at the organismal level upon stress.

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Biological resilience and aging: Activation of stress response pathways contributes to lifespan extension

Soo

Rudich

et al. 2023

Ageing Research Reviews

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HSF-1 displays nuclear stress body formation in multiple tissues in Caenorhabditis elegans upon stress and following the transition to adulthood

Cited by 10 publications

References 47 publications

HSF-1: Guardian of the Proteome Through Integration of Longevity Signals to the Proteostatic Network

HSF-1: Guardian of the Proteome Through Integration of Longevity Signals to the Proteostatic Network

The CBP-1/p300 Lysine Acetyltransferase Regulates the Heat Shock Response in C. elegans

Biological resilience and aging: Activation of stress response pathways contributes to lifespan extension

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