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RSK2 represses HSF1 activation during heat shock

X Wang1, A Asea, Y Xie

  • 1Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.

Cell Stress & Chaperones
|February 24, 2001
PubMed

Insights

Heat shock transcription factor 1 (HSF1) activation is regulated by the protein kinase RSK2. RSK2 represses HSF1 DNA binding activity, particularly during heat shock, as shown in Coffin-Lowry syndrome cells lacking RSK2.

Area of Science:

  • Molecular Biology
  • Cellular Stress Response

Background:

  • Heat shock transcription factor 1 (HSF1) activation is a complex process involving its translocation to the nucleus and DNA binding.
  • Nonsteroidal anti-inflammatory drugs (NSAIDs) have been shown to activate HSF1.
  • Previous research indicated that RSK2 phosphorylates HSF1 in vitro, an effect inhibited by NSAIDs.

Purpose of the Study:

  • To investigate the role of RSK2 in HSF1 activation in vivo.
  • To examine HSF1 activation in cells deficient in RSK2, specifically in the context of Coffin-Lowry syndrome.

Main Methods:

  • Utilized cell lines from a patient with Coffin-Lowry syndrome (RSK2 deficient).
  • Assessed HSF1-HSE DNA binding activity following treatment with sodium salicylate and heat shock.
  • Compared HSF1 activation in Coffin-Lowry syndrome cells versus normal control cells.

Main Results:

  • RSK2 slightly represses HSF1 activation in vivo at 37°C.
  • HSF1-HSE DNA binding activity was slightly elevated in Coffin-Lowry syndrome cells after sodium salicylate treatment compared to untreated cells.
  • Heat shock treatment induced significantly higher HSF1-HSE binding activity in Coffin-Lowry syndrome cells than in normal controls.

Conclusions:

  • RSK2 plays a role in repressing HSF1-HSE DNA binding activity, especially during heat shock.
  • While RSK2 is involved in HSF1 regulation, it is not the sole protein kinase suppressing HSF1-HSE binding at 37°C.
  • These findings highlight RSK2 as a key repressor of HSF1 activity under thermal stress.

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