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Heat Shock Transcription Factors: Structure and Regulation
Abstract
Organisms respond to elevated temperatures and to chemical and physiological stresses by an increase in the synthesis of heat shock proteins. The regulation of heat shock gene expression in eukaryotes is mediated by the conserved heat shock transcription factor (HSF). HSF is present in a latent state under normal conditions; it is activated upon heat stress by induction of trimerization and high-affinity binding to DNA and by exposure of domains for transcriptional activity. Analysis of HSF cDNA clones from many species has defined structural and regulatory regions responsible for the inducible activities. The heat stress signal is thought to be transduced to HSF by changes in the physical environment, in the activity of HSF-modifying enzymes. or by changes in the intracellular level of heat shock proteins.
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“HSP90 transcription is controlled by the heat shock transcription factor HSF, a key regulator of the heat shock response36,37 that is evolutionarily conserved from S. cerevisiae (Hsf1) to mammals (HSF1/2).”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [37]
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Morimoto, R. I. (1998) · Genes & Development · doi:10.1101/gad.12.24.3788 · Cited by 1,898
Heat shock factors: integrators of cell stress, development and lifespan
Åkerfelt, M., Morimoto, R. I., & Sistonen, L. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2938 · Cited by 1,516
“Subsequent studies showed that, in contrast to a single HSF in invertebrates, multiple HSFs are expressed in plants and vertebrate”
Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications
Ciocca, D. R., & Calderwood, S. K. (2005) · Cell Stress and Chaperones · doi:10.1379/csc-99r.1 · Cited by 1,420
“Hsp transcription requires activated heat shock transcription factor 1 (hsf1), which is itself overexpressed in cancer and plays a role in invasion and metastasis (Wu 1995; McMillan et al 1998; Hoang et al 2000; Wang et al 2004).”
BackgroundRole of the Heat Shock Response and Molecular Chaperones in Oncogenesis and Cell Death
Jolly, C. (2000) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/92.19.1564 · Cited by 1,052
The 90-kDa Molecular Chaperone Family
Csermely, P., Schnaider, T., Sőti, C., Prohászka, Z., & Nardai, G. (1998) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(98)00013-8 · Cited by 1,024
Metadata
- Authors
- Wu, C.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Wu, Carl
- ORCID
- Wu, Carl
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 1995-11
- Volume
- 11
- Issue
- 1
- Pages
- 441-469
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2145760315
- Cited by
- 1,231
- References
- 0
- Citations by year
- 2026: 13 · 2025: 23 · 2024: 29 · 2023: 20 · 2022: 32 · 2021: 33 · 2020: 23 · 2019: 35 · 2018: 35 · 2017: 31 · 2016: 40 · 2015: 48 · 2014: 44 · 2013: 49 · 2012: 57
- FWCI
- 11.93
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- heat shock transcription factor, heat shock proteins, heat shock gene expression, DNA binding, transcriptional activation
- MeSH terms
- Heat Shock Transcription Factors, Amino Acid Sequence, Animals, Bacteria, Binding Sites, Cloning, Molecular, DNA-Binding Proteins, Heat-Shock Proteins, Humans, Models, Structural, Molecular Sequence Data, Transcription Factors, Conserved Sequence, Sequence Homology, Amino Acid, Protein Structure, Secondary, Helix-Turn-Helix Motifs
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