ArticleMolecular and cellular biology2000
Disruption of heat shock factor 1 reveals an essential role in the ubiquitin proteolytic pathway.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 120 citations in OpenAlex.
- The ubiquitin-proteasome system and proteostasis in the cochlea and sensorineural hearing disorders.Molecular biomedicine · 2026Review
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- Multiplexed dynamic control of temperature to probe and observe mammalian cells.bioRxiv : the preprint server for biology · 2024Article
- Editing ofAnimal biotechnology · 2023Article
- HSF1 and Its Role in Huntington's Disease Pathology.Advances in experimental medicine and biology · 2023Review
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- The proteostasis guardian HSF1 directs the transcription of its paralog and interactor HSF2 during proteasome dysfunction.Cellular and molecular life sciences : CMLS · 2021Article
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- Proteostasis Regulation in the Endoplasmic Reticulum: An Emerging Theme in the Molecular Pathology and Therapeutic Management of Familial Hypercholesterolemia.Frontiers in genetics · 2020Review
- Roles of heat shock factor 1 beyond the heat shock response.Cellular and molecular life sciences : CMLS · 2018Review
- NEDD4-mediated HSF1 degradation underlies α-synucleinopathy.Human molecular genetics · 2016Article
- Proteotoxic stress reprograms the chromatin landscape of SUMO modification.Science signaling · 2015Article
- Polymorphisms in human heat shock factor-1 and analysis of potential biological consequences.Cell stress & chaperones · 2015Article
- Celastrol, an oral heat shock activator, ameliorates multiple animal disease models of cell death.Cell stress & chaperones · 2015Article
- The proteasome inhibitor bortezomib is a potent inducer of zinc finger AN1-type domain 2a gene expression: role of heat shock factor 1 (HSF1)-heat shock factor 2 (HSF2) heterocomplexes.The Journal of biological chemistry · 2014Article
- Late-onset Alzheimer's disease, heating up and foxed by several proteins: pathomolecular effects of the aging process.Journal of Alzheimer's disease : JAD · 2014Article
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- The ubiquitin-proteasome system in retinal health and disease.Molecular neurobiology · 2013Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Inhibition of proteasome-mediated protein degradation machinery is a potent stress stimulus that causes accumulation of ubiquitinated proteins and increased expression of heat shock proteins (Hsps). Hsps play pivotal roles in homeostasis and protection in a cell, through their well-recognized properties as molecular chaperones. The inducible Hsp expression is regulated by the heat shock transcription factors (HSFs). Among mammalian HSFs, HSF1 has been shown to be important for regulation of the heat-induced stress gene expression, whereas the function of HSF2 in stress response is unclear. Recent reports have suggested that both HSF1 and HSF2 are affected during down-regulation of ubiquitin-proteasome pathway (Y. Kawazoe et al., Eur. J. Biochem. 255:356-362, 1998; A. Mathew et al., Mol. Cell. Biol. 18:5091-5098, 1998; D. Kim et al., Biochem. Biophys. Res. Commun. 254:264-268, 1999). To date, however, no unambiguous evidence has been presented as to whether a single specific HSF or multiple members of the HSF family are required for transcriptional induction of heat shock genes when proteasome activity is down-regulated. Therefore, by using loss-of-function and gain-of-function strategies, we investigated the specific roles of mammalian HSFs in regulation of the ubiquitin-proteasome-mediated stress response. Here we demonstrate that HSF1, but not HSF2, is essential and sufficient for up-regulation of Hsp70 expression during down-regulation of the ubiquitin proteolytic pathway. We propose that specificity of HSF1 could be an important therapeutic target during disease pathogenesis associated with abnormal ubiquitin-dependent proteasome function.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.