Rethinking HSF1 in Stress, Development, and Organismal Health

Li, Jian; Labbadia, Johnathan; Morimoto, Richard I.

doi:10.1016/j.tcb.2017.08.002

Cited by 221 publications

(223 citation statements)

References 65 publications

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“…An important distinction shown here is that mitochondrial perturbation also maintains the HSR and cytosolic proteostasis with age. Given that the transcription factor HSF-1 is central to the HSR, stress resistance, and cytosolic proteostasis (Akerfelt et al, 2010; Li, Labbadia and Morimoto, 2017), we asked whether the beneficial effects of mitochondrial stress require HSF-1. Therefore, we examined survival following HS in animals exposed to L4440 or F29C4.2(0.2)(RNAi) in combination with hsf-1(RNAi) or atfs-1(RNAi) , and in hsf-1(sy441) and atfs-1(tm4525) mutants that have a diminished HSR and UPR mt respectively (Bennett et al, 2014; Li et al, 2016; Nargund et al., 2015).…”

Section: Resultsmentioning

confidence: 99%

Mitochondrial Stress Restores the Heat Shock Response and Prevents Proteostasis Collapse during Aging

et al. 2017

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Summary In Caenorhabditis elegans, the programmed repression of the heat shock response (HSR) accompanies the transition to reproductive maturity, leaving cells vulnerable to environmental stress and protein aggregation with age. To identify the factors driving this event, we performed an unbiased genetic screen for suppressors of stress resistance, and identified the mitochondrial electron transport chain (ETC) as a central regulator of the age-related decline of the HSR and cytosolic proteostasis. Mild down-regulation of ETC activity, either by genetic modulation or exposure to mitochondria targeted xenobiotics, maintained the HSR in adulthood by increasing HSF-1 binding and RNA polymerase II recruitment at HSF-1 target genes. This resulted in a robust restoration of cytoplasmic proteostasis and increased vitality later in life, without detrimental effects on fecundity. We propose that low levels of mitochondrial stress regulate cytoplasmic proteostasis and healthspan during aging by coordinating the long-term activity of HSF-1 with conditions preclusive to optimal fitness.

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Section: Resultsmentioning

confidence: 99%

Mitochondrial Stress Restores the Heat Shock Response and Prevents Proteostasis Collapse during Aging

et al. 2017

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“…21,22 Heat shock factor 1 is also activated in breast cancer tissue, and its high expression level is associated with poor prognosis of breast cancer. 21,22 Heat shock factor 1 is also activated in breast cancer tissue, and its high expression level is associated with poor prognosis of breast cancer.…”

Section: Introductionmentioning

confidence: 99%

FAM3C‐YY1 axis is essential for TGFβ‐promoted proliferation and migration of human breast cancer MDA‐MB‐231 cells via the activation of HSF1

Yang

Feng

Meng

et al. 2019

J Cellular Molecular Medi

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Family with sequence similarity three member C (FAM3C) (interleukin‐like EMT inducer [ILEI]), heat shock factor 1 (HSF1) and Ying‐Yang 1 (YY1) have been independently reported to be involved in the pathogenesis of various cancers. However, whether they are coordinated to trigger the development of cancer remains unknown. This study determined the role and mechanism of YY1 and HSF1 in FAM3C‐induced proliferation and migration of breast cancer cells. In human MDA‐MB‐231 breast cancer cell line, transforming growth factor‐β (TGFβ) up‐regulated FAM3C, HSF1 and YY1 expressions. FAM3C overexpression promoted the proliferation and migration of MDA‐MB‐231 cells with YY1 and HSF1 up‐regulation, whereas FAM3C silencing exerted the opposite effects. FAM3C inhibition repressed TGFβ‐induced HSF1 activation, and proliferation and migration of breast cancer cells. YY1 was shown to directly activate HSF1 transcription to promote the proliferation and migration of breast cancer cells. YY1 silencing blunted FAM3C‐ and TGFβ‐triggered activation of HSF1‐Akt‐Cyclin D1 pathway, and proliferation and migration of breast cancer cells. Inhibition of HSF1 blocked TGFβ‐, FAM3C‐ and YY1‐induced proliferation and migration of breast cancer cells. YY1 and HSF1 had little effect on FAM3C expression. Similarly, inhibition of HSF1 also blunted FAM3C‐ and TGFβ‐promoted proliferation and migration of human breast cancer BT‐549 cells. In human breast cancer tissues, FAM3C, YY1 and HSF1 protein expressions were increased. In conclusion, FAM3C activated YY1‐HSF1 signalling axis to promote the proliferation and migration of breast cancer cells. Furthermore, novel FAM3C‐YY1‐HSF1 pathway plays an important role in TGFβ‐triggered proliferation and migration of human breast cancer MDA‐MB‐231 cells.

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“…Thus, HSF1 directs transcriptional programs distinct from the heat shock response during cell proliferation, differentiation, and aging [3,5]. Thus, HSF1 directs transcriptional programs distinct from the heat shock response during cell proliferation, differentiation, and aging [3,5].…”

Section: Introductionmentioning

confidence: 99%

“…Heat shock factor HSF1 is the major transcriptional regulator of HSP genes [2,3]. HSF1 interacts with the general transcription factors and Mediator to induce Pol II release/elongation and reinitiation [2,3]. Upon heat shock, the activity of HSF1 is strongly influenced by post-translational modifications, and transcriptionally active HSF1 binds to the heat shock element (HSE) in the promoter.…”

Section: Introductionmentioning

confidence: 99%

“…The heat shock response involves rapid and robust induction of heat shock proteins (HSPs), also known as molecular chaperones, and protects cells from the proteotoxic environment of thermal stress. Heat shock factor HSF1 is the major transcriptional regulator of HSP genes [2,3]. Promoter-proximal pausing of RNA polymerase II (Pol II) is a widespread regulatory mechanism in gene expression, including HSP genes [4].…”

Section: Introductionmentioning

confidence: 99%

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TAF7 is a heat‐inducible unstable protein and is required for sustained expression of heat shock protein genes

et al. 2018

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TATA-binding protein-associated factor 7 (TAF7), a dissociable component of the general transcription factor IID (TFIID), plays a role as a check-point regulator at the step of RNA polymerase II (Pol II) transcription initiation. Here, we focused on the role of TAF7 in heat-shocked cells, where its expression is induced by heat shock factor HSF1. TAF7 is a phosphoprotein, and the phosphorylation status is related to its interaction with TFIID and to its stability controlled by the ubiquitin-proteasome pathway. TAF7 is necessary for the prolonged expression of heat shock protein genes and for efficient recovery of heat-shocked cells. During sustained transcription, TAF7, presumably its TFIID-independent form, binds the promoter and enhances the levels of Pol II at the gene body but not the promoter. These results showed the novel function of TAF7 that is necessary for the transition from initiation to elongation in multiple-round transcription.

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Rethinking HSF1 in Stress, Development, and Organismal Health

Cited by 221 publications

References 65 publications

Mitochondrial Stress Restores the Heat Shock Response and Prevents Proteostasis Collapse during Aging

Mitochondrial Stress Restores the Heat Shock Response and Prevents Proteostasis Collapse during Aging

FAM3C‐YY1 axis is essential for TGFβ‐promoted proliferation and migration of human breast cancer MDA‐MB‐231 cells via the activation of HSF1

TAF7 is a heat‐inducible unstable protein and is required for sustained expression of heat shock protein genes

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