ArticleMolecular and cellular biology1995
The carboxyl-terminal transactivation domain of heat shock factor 1 is negatively regulated and stress responsive.
Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 128 citations in OpenAlex.
- Adaptation to heat stress by diversification of the vertebrate heat shock transcription factor family.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Role of HSF1 in cell division, tumorigenesis and therapy: a literature review.Cell division · 2025Review
- HSF1 is required for cellular adaptation to daily temperature fluctuations.Scientific reports · 2024Article
- The pericentromeric protein shugoshin 2 cooperates with HSF1 in heat shock response and RNA Pol II recruitment.The EMBO journal · 2019Article
- Article
- Tailoring of Proteostasis Networks with Heat Shock Factors.Cold Spring Harbor perspectives in biology · 2019Review
- HSP90 inhibitors disrupt a transient HSP90-HSF1 interaction and identify a noncanonical model of HSP90-mediated HSF1 regulation.Scientific reports · 2018Article
- The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status.Molecular cell · 2012Article
- Small molecule activators of the heat shock response: chemical properties, molecular targets, and therapeutic promise.Chemical research in toxicology · 2012Review
- Functional analysis of the Hsf4(lop11) allele responsible for cataracts in lop11 mice.Molecular vision · 2011Article
- Heat shock factors: integrators of cell stress, development and lifespan.Nature reviews. Molecular cell biology · 2010Review
- A novel mouse HSF3 has the potential to activate nonclassical heat-shock genes during heat shock.Molecular biology of the cell · 2010Article
- PDSM, a motif for phosphorylation-dependent SUMO modification.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Heat shock-independent induction of multidrug resistance by heat shock factor 1.Molecular and cellular biology · 2006Article
- Article
- On mechanisms that control heat shock transcription factor activity in metazoan cells.Cell stress & chaperones · 2004Review
- Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1.Molecular and cellular biology · 2003Article
- Dynamic association of transcriptional activation domains and regulatory regions in Saccharomyces cerevisiae heat shock factor.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Stress-specific activation and repression of heat shock factors 1 and 2.Molecular and cellular biology · 2001Article
- Phosphorylation of serine 230 promotes inducible transcriptional activity of heat shock factor 1.The EMBO journal · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have characterized a stress-responsive transcriptional activation domain of mouse heat shock factor 1 (HSF1) by using chimeric GAL4-HSF1 fusion proteins. Fusion of the GAL4 DNA-binding domain to residues 124 to 503 of HSF1 results in a chimeric factor that binds DNA yet lacks any transcriptional activity. Transactivation is acquired upon exposure to heat shock or by deletion of a negative regulatory domain including part of the DNA-binding-domain-proximal leucine zippers. Analysis of a collection of GAL4-HSF1 deletion mutants revealed the minimal region for the constitutive transcriptional activator to map within the extreme carboxyl-terminal 108 amino acids, corresponding to a region rich in acidic and hydrophobic residues. Loss of residues 395 to 425 or 451 to 503, which are located at either end of this activation domain, severely diminished activity, indicating that the entire domain is required for transactivation. The minimal activation domain of HSF1 also confers enhanced transcriptional response to heat shock or cadmium treatment. These results demonstrate that the transcriptional activation domain of HSF1 is negatively regulated and that the signal for stress induction is mediated by interactions between the amino-terminal negative regulator and the carboxyl-terminal transcriptional activation domain.
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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.