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Growth factor-induced activation of MSK2 leads to phosphorylation of H3K9me2S10 and corresponding changes in gene

Karen G Wong1, Yu-Chia F Cheng1, Vincent H Wu2

  • 1Department of Cell and Developmental Biology, Penn Epigenetics Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

Science Advances
|March 13, 2024
PubMed

Insights

Growth factors trigger epigenetic changes, specifically histone H3 phosphorylation (H3K9me2S10ph), to control gene expression. This modification, mediated by MSK2 kinase, is crucial for activating EGF-responsive genes.

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Cell Signaling

Background:

  • Extracellular signals regulate gene expression via kinase cascades.
  • The role of epigenetic modifications in this process is not fully understood.

Purpose of the Study:

  • To investigate the link between growth factor signaling and epigenetic changes.
  • To identify specific histone modifications involved in regulating gene expression.

Main Methods:

  • Utilized imaging and proteomic approaches.
  • Analyzed histone phosphorylation levels, specifically H3K9me2S10ph.
  • Investigated the role of the nuclear kinase MSK2.

Main Results:

  • Epidermal growth factor (EGF) stimulation increases H3K9me2S10ph in regulatory regions of EGF-responsive genes.
  • EGF-induced H3K9me2S10ph is dependent on the nuclear kinase MSK2.
  • MSK2 is essential for the transcription of a subset of EGF-induced genes.

Conclusions:

  • Growth factor-induced chromatin state changes mediate downstream gene activation.
  • Histone phosphorylation, specifically H3K9me2S10ph, is a key epigenetic mechanism in growth factor signaling.
  • MSK2 plays a critical role in mediating the transcriptional response to EGF.

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