Evidence map›Paper›PMID 11585899›Full record

ArticleMolecular and cellular biology2001

Stress-specific activation and repression of heat shock factors 1 and 2.

A Mathew, S K Mathur, C Jolly, S G Fox, S Kim, R I Morimoto

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed.

  1. Review
  2. The Function of Heat Shock Transcription Factors in Sex Differentiation inAnimals : an open access journal from MDPI · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

A MathewDepartment of Biochemistry, Molecular Biology, and Cell Biology, Rice Institute for Biomedical Research, Northwestern University, Evanston, Illinois 60208, USA.
S K Mathur
C Jolly
S G Fox
S Kim
R I Morimoto

Funding

REGULATION AND EXPRESSION OF THE HSP70 GENE FAMILYR37GM038109 · NIGMS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2000 to 2009
$5.6M
REGULATION AND EXPRESSION OF THE HUMAN HSP70 GENE FAMILYR01GM038109 · NIGMS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 1987 to 2013
$2.2M
NIGMS NIH HHS GM38109NIGMS NIH HHS R01 GM038109NIGMS NIH HHS R37 GM038109
6 · The paper itself

Abstract

Vertebrate cells express a family of heat shock transcription factors (HSF1 to HSF4) that coordinate the inducible regulation of heat shock genes in response to diverse signals. HSF1 is potent and activated rapidly though transiently by heat shock, whereas HSF2 is a less active transcriptional regulator but can retain its DNA binding properties for extended periods. Consequently, the differential activation of HSF1 and HSF2 by various stresses may be critical for cells to survive repeated and diverse stress challenges and to provide a mechanism for more precise regulation of heat shock gene expression. Here we show, using a novel DNA binding and detection assay, that HSF1 and HSF2 are coactivated to different levels in response to a range of conditions that cause cell stress. Above a low basal activity of both HSFs, heat shock preferentially activates HSF1, whereas the amino acid analogue azetidine or the proteasome inhibitor MG132 coactivates both HSFs to different levels and hemin preferentially induces HSF2. Unexpectedly, we also found that heat shock has dramatic adverse effects on HSF2 that lead to its reversible inactivation coincident with relocalization from the nucleus. The reversible inactivation of HSF2 is specific to heat shock and does not occur with other stressors or in cells expressing high levels of heat shock proteins. These results reveal that HSF2 activity is negatively regulated by heat and suggest a role for heat shock proteins in the positive regulation of HSF2.

Indexed as

3T3 CellsAnimalsBlotting, WesternCell NucleusCytoplasmDNADNA-Binding ProteinsEnzyme ActivationHeat-Shock ProteinsHeat Shock Transcription FactorsMiceMicroscopy, FluorescenceModels, BiologicalProtein BindingTranscription FactorsTranscription, GeneticDNADNA-Binding ProteinsHeat-Shock ProteinsHeat Shock Transcription FactorsHSF1 protein, humanHSF2 protein, humanTranscription Factors

Identifiers

PMID11585899
PMCPMC99891

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.