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Crosstalk between p38 and Erk 1/2 in Downregulation of FGF1-Induced Signaling

Malgorzata Zakrzewska1, Lukasz Opalinski2, Ellen M Haugsten3,4

  • 1Department of Protein Engineering, Faculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland. malgorzata.zakrzewska@uwr.edu.pl.

International Journal of Molecular Sciences
|April 25, 2019
PubMed

Insights

Mitogen-activated protein kinases (MAPK), Erk1 and Erk2, regulate fibroblast growth factor (FGF) signaling. Novel crosstalk between p38 and Erk1/2 kinases in FGF signaling downregulation was discovered.

Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Signal transduction

Background:

  • Mitogen-activated protein kinases (MAPK), specifically Erk1 and Erk2, are crucial for the negative feedback regulation of fibroblast growth factor (FGF) signaling.
  • Erk1 and Erk2 phosphorylate FGF receptor 1 (FGFR1) and FGF receptor substrate 2 (FRS2), reducing receptor signaling.

Purpose of the Study:

  • To investigate the role of p38 kinase in FGF signaling.
  • To elucidate the interplay between p38 and Erk1/2 kinases in regulating FGF-induced signaling.

Main Methods:

  • Utilized NIH3T3 mouse fibroblasts and human osteosarcoma U2OS cells stably expressing FGFR1.
  • Employed kinase inhibitors for Erk1/2 and p38.
  • Analyzed phosphorylation patterns of FGFR1 and FRS2.
  • Stimulated p38 activity using anisomycin.

Main Results:

  • Demonstrated that p38 kinase, in addition to Erk1/2, phosphorylates FRS2.
  • Simultaneous inhibition of Erk1/2 and p38 kinases resulted in prolonged tyrosine phosphorylation of FGFR1 and FRS2, leading to sustained signaling.
  • Excessive activation of p38 partially compensated for the lack of Erk activity.

Conclusions:

  • Revealed a novel crosstalk between p38 and Erk1/2 kinases in the downregulation of FGF-induced signaling.
  • p38 kinase plays a significant role in modulating FGF signaling.
Keywords:
FGF-induced signalingFRS2MAPKdownregulationp38phosphorylation

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