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MSK1 is required for CREB phosphorylation in response to mitogens in mouse embryonic stem cells

J S Arthur1, P Cohen

  • 1MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dow Street, Dundee DD1 5EH, UK. j.s.c.arthur@dundee.ac.uk

FEBS Letters
|October 6, 2000
PubMed

Insights

Mitogen- and stress-activated protein kinase 1 (MSK1) is essential for phosphorylating CREB and ATF1 in mouse embryonic stem cells upon stimulation. Its absence prevents this critical phosphorylation pathway, impacting cellular responses.

Area of Science:

  • Cellular signaling pathways
  • Stem cell biology
  • Molecular mechanisms of gene regulation

Background:

  • Mitogen- and stress-activated protein kinase 1 (MSK1) plays a role in cellular responses to stimuli.
  • Extracellular signal-regulated kinases (ERK1/ERK2) are key activators in signaling cascades.
  • Cyclic AMP-responsive element binding protein (CREB) and ATF1 are transcription factors involved in gene expression.

Purpose of the Study:

  • To investigate the role of MSK1 in the phosphorylation of CREB and ATF1 in mouse embryonic stem cells.
  • To determine if MSK1 is required for mitogen- and stress-induced phosphorylation of these transcription factors.

Main Methods:

  • Generation of MSK1 knockout (MSK1-/-) mouse embryonic stem cells.
  • Stimulation of cells with tetradecanoylphorbol acetate (TPA) and epidermal growth factor (EGF).
  • Analysis of protein phosphorylation using Western blotting and kinase assays.

Main Results:

  • MSK1-/- cells showed no detectable MSK1 activity, but ERK1/ERK2 activation was normal.
  • TPA and EGF induced CREB/ATF1 phosphorylation at specific sites in wild-type cells, which was abolished in MSK1-/- cells.
  • Basal and forskolin-induced phosphorylation remained unaffected in MSK1-/- cells, indicating MSK1's specific role in mitogenic signaling.

Conclusions:

  • MSK1 is indispensable for the phosphorylation of CREB and ATF1 in response to mitogenic stimuli in mouse embryonic stem cells.
  • The findings highlight MSK1's critical role in linking extracellular signals to transcription factor activation in stem cells.

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