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Updated: Jul 3, 2026
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Measurements of Physiological Stress Responses in C. Elegans
Published on: May 21, 2020
CoREST represses the heat shock response mediated by HSF1
Andrea V Gómez1, Danny Galleguillos, Juan Cristóbal Maass
1Millenium Nucleus in Stress and Addiction, Departamento de Biología Celular y Molecular, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago 8330025, Chile.
Molecular Cell
|July 29, 2008
Summary
The corepressor CoREST interacts with Hsp70, repressing heat shock gene activation. Reducing CoREST impairs Hsp70
Area of Science:
- Molecular Biology
- Cellular Stress Response
Background:
- Cellular stress response involves rapid transcriptional activation of stress genes.
- Heat shock protein 70 (Hsp70) acts as a corepressor for heat shock factor 1 (HSF1) during stress response attenuation.
Purpose of the Study:
- To investigate the interaction between CoREST and Hsp70.
- To determine CoREST's role in regulating HSF1-dependent transcription of the hsp70 promoter.
Main Methods:
- Investigated CoREST-Hsp70 interaction.
- Utilized short hairpin RNAs (shRNAs) to reduce CoREST levels.
- Performed chromatin immunoprecipitation (ChIP) assays.
Main Results:
- CoREST interacts with Hsp70 and represses hsp70 promoter activity.
- Reduced CoREST levels abolished Hsp70's corepression of HSF1-dependent transcription.
- Lowered CoREST levels increased Hsp70 protein and HSF1-dependent transactivation.
- CoREST binds to the hsp70 promoter, with increased binding during heat shock.
Conclusions:
- CoREST is a key regulator of the heat shock stress response.
- CoREST mediates Hsp70's role in repressing HSF1-dependent transcription.
- CoREST functions by binding to the hsp70 gene promoter.
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