Heat shock factor 1 is inactivated by amino acid deprivation

Hensen, Sanne M. M.; Heldens, Lonneke; Enckevort, Chrissy M. W. van; Genesen, Siebe T. van; Pruijn, Ger J. M.; Lubsen, Nicolette H.

doi:10.1007/s12192-012-0347-1

Cited by 32 publications

(33 citation statements)

References 37 publications

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“…AMPK can also regulate the HSR indirectly through its substrate PGC1α, a regulator of mitochondrial biogenesis that interacts with HSF1 during fasting in mouse livers and primary hepatocytes [17], thereby repressing the HSR when energy availability is low. Furthermore, HSF1 is inactivated by amino acid deprivation [32]. A potential mechanism involves mTORC1, a key regulator of translation that depends on amino acid levels, which promotes HSF1 activity through phosphorylation at Ser326 [33].…”

Section: Regulation Of Hsf1 By the Proliferative And Metabolic Statesmentioning

confidence: 99%

Rethinking HSF1 in Stress, Development, and Organismal Health

Labbadia

Morimoto

2017

Trends in Cell Biology

225

210

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The heat shock response (HSR) was originally discovered as a transcriptional response to elevated temperature shock and led to the identification of heat shock proteins and Heat Shock Factor 1 (HSF1). Since then, HSF1 has been shown to be important for combating other forms of environmental perturbations as well as genetic variations that cause proteotoxic stress. The HSR has long been thought to be an absolute response to conditions of cell stress and the primary mechanism by which HSF1 promotes organismal health by preventing protein aggregation and subsequent proteome imbalance. Accumulating evidence now shows that HSF1, the central player in the HSR, is regulated according to specific cellular requirements through cell-autonomous and non-autonomous signals, and directs transcriptional programs distinct from the HSR during development and in carcinogenesis. Here, we discuss these ‘non-canonical’ roles of HSF1, and its regulation in diverse conditions of development, reproduction, metabolism, and aging, and posit that HSF1 serves to integrate diverse biological and pathological responses.

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Section: Regulation Of Hsf1 By the Proliferative And Metabolic Statesmentioning

confidence: 99%

Rethinking HSF1 in Stress, Development, and Organismal Health

Labbadia

Morimoto

2017

Trends in Cell Biology

225

210

View full text Add to dashboard Cite

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“…The significant increase of plasma BHBA in response to LPD is the biochemical result of the physiological imbalance of the experimental cows and strengthens the power of O 2 P-HR method as a reliable measure of the energy status. (Hensen et al 2011). In a recent study, we showed that while Hsp70 attenuated in mammary gland epithelial cells, in response to caloric stress, FABP3 levels increased (Eitam et al 2009).…”

Section: Biochemical Indications For the Negative Energy Statusmentioning

confidence: 87%

Protein deprivation attenuates Hsp expression in fat tissue

Eitam

Agmon

Asher

et al. 2012

Cell Stress and Chaperones

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For ruminants, dietary protein is the first limiting component to the utilization of low-quality forage. Throughout gestation, low-protein intake may result in prenatal programming that causes various metabolic disturbances and physiological modulations to dams and their developing embryos. We studied the effect of long-term low-protein diet (LPD) on physiological, biochemical, and molecular parameters of the energy status in gestating beef cows. LPD resulted in significant reductions in feed intake and heart rate and promoted a negative retained energy status already after 3 weeks. Elevated levels of plasma creatinine and non-esterified fatty acids indicate endogenous degradation of fat and protein as a response to the demands in energy and nitrogen. Increasing levels of β-hydroxybutyrate confirmed the negative energy status obtained by the physiological measurements. At the molecular level, subcutaneous fat, Hsp90, Hsp70, and proteasome subunits decreased significantly after 3 months on LPD, in parallel with an increase of adipocyte fatty acidbinding protein. These results may indicate a decrease in turn-over of proteins, at the cost of induced lipolysis, and suggest that the response to protein deprivation, when examined in an energy-storing tissue, includes downregulation of the constitutive heat shock proteins involved in the protein degradation pathway of energy production and upregulation of tissue-specific genes such as those involved in energy production from fat degradation.

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“…In calorie-restricted cells, the age-related diminishment of HSF1 DNA binding is reversed [87]. Contrary to calorie restriction, amino acid deprivation impairs HSF1 DNA-binding activity and suppresses the expression of HSP mRNAs [88]. Similarly, depletion of glutathione also suppresses the HSF1 activation by heat shock [89].…”

Section: Metabolic Control Of the Psr In Diabetes Mellitusmentioning

confidence: 99%

Metabolic control of the proteotoxic stress response: implications in diabetes mellitus and neurodegenerative disorders

Dai

2016

Cell. Mol. Life Sci.

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Proteome homeostasis, or proteostasis, is essential to maintain cellular fitness and its disturbance is associated with a broad range of human health conditions and diseases. Cells are constantly challenged by various extrinsic and intrinsic insults, which perturb cellular proteostasis and provoke proteotoxic stress. To counter proteomic perturbations and preserve proteostasis, cells mobilize the proteotoxic stress response (PSR), an evolutionarily conserved transcriptional program mediated by heat shock factor 1 (HSF1). The HSF1-mediated PSR guards the proteome against misfolding and aggregation. In addition to proteotoxic stress, emerging studies reveal that this proteostatic mechanism also responds to cellular energy state. This regulation is mediated by. In this review, we present an overview of the maintenance of proteostasis by HSF1, the metabolic regulation of the PSR, particularly focusing on the key cellular metabolic sensor AMP-activated protein kinase (AMPK), and their implications in the two major age-related diseases—diabetes mellitus and neurodegenerative disorders.

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Heat shock factor 1 is inactivated by amino acid deprivation

Cited by 32 publications

References 37 publications

Rethinking HSF1 in Stress, Development, and Organismal Health

Rethinking HSF1 in Stress, Development, and Organismal Health

Protein deprivation attenuates Hsp expression in fat tissue

Metabolic control of the proteotoxic stress response: implications in diabetes mellitus and neurodegenerative disorders

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