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Repression motif in HSF1 regulated by phosphorylation.

Stefan Gabriel1, Thomas Czerny1, Elisabeth Riegel1

  • 1Department of Applied Life Sciences, University of Applied Sciences, FH Campus Wien, Favoritenstraße 222, A-1100 Vienna, Austria.

Cellular Signalling
|July 19, 2023
PubMed
Summary
This summary is machine-generated.

Heat shock factor 1 (HSF1) activation is regulated by phosphorylation. This study identifies a specific phosphorylation site (S303) on HSF1 that represses its transcriptional activity, revealing a novel repression mechanism.

Keywords:
HSF1Heat shock factorPhosphorylationReporter assayRepression

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Area of Science:

  • Molecular Biology
  • Cellular Stress Response

Background:

  • Heat shock factor 1 (HSF1) is a key transcription factor orchestrating the cellular heat shock response (HSR) to proteotoxic stress.
  • While HSF1 activation is crucial for cell survival, its precise regulatory mechanisms, particularly the role of phosphorylation, remain incompletely understood.

Purpose of the Study:

  • To investigate the role of HSF1 phosphorylation in regulating its transcriptional activity.
  • To identify specific phosphorylation sites and motifs responsible for HSF1 activation or repression.

Main Methods:

  • Mutagenesis of HSF1 at known phosphorylation sites to create phosphor-mimicking (11 M(+)) and phosphor-diminishing (11 M(-)) variants.
  • Assaying transactivation potential using an HSR reporter plasmid under various stress conditions.
  • Analyzing the effect of single amino acid substitutions, particularly at the S303/307 motif.

Main Results:

  • HSF1 activation by heat is independent of phosphorylation.
  • Distinct cellular stresses differentially affect the activation potential of HSF1 variants.
  • Phosphorylation at serine 303 (S303) was identified as solely responsible for repressing HSF1 activity.
  • A small repressive motif, independent of HSF1 context, was found to downregulate promoter transcription.

Conclusions:

  • HSF1 phosphorylation, particularly at S303, plays a critical role in modulating its transcriptional output.
  • A novel mechanism of HSF1 repression involves a small motif that directly impacts promoter activity, beyond previously known pathways.