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Fibroblast growth factor receptor 2 phosphorylation on serine 779 couples to 14-3-3 and regulates cell survival and

Ana Lonic1, Emma F Barry, Cindy Quach

  • 1Division of Human Immunology, Institute of Medical and Veterinary Science, Frome Rd. Adelaide, South Australia, Australia.

Molecular and Cellular Biology
|March 12, 2008
PubMed

Insights

Fibroblast Growth Factor Receptor 2 (FGFR2) uses serine 779 phosphorylation to activate 14-3-3 proteins, enhancing cell survival and proliferation signaling pathways. This discovery reveals a new mechanism for regulating diverse biological responses.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Fibroblast Growth Factors (FGFs) mediate diverse biological responses via Fibroblast Growth Factor Receptors (FGFRs).
  • FGFRs initiate intracellular signaling through receptor tyrosine phosphorylation, but mechanisms for pleiotropic responses remain unclear.

Purpose of the Study:

  • To identify a novel mechanism by which FGFR2 regulates intracellular signaling and cellular responses.
  • To elucidate the role of FGFR2 serine 779 phosphorylation in FGF2-mediated signaling.

Main Methods:

  • Investigated FGFR2 phosphorylation on serine 779 (S779) in response to FGF2.
  • Assessed the interaction of phosphorylated S779 with 14-3-3 proteins.
  • Analyzed the activation of phosphatidylinositol 3-kinase and Ras/mitogen-activated protein kinase pathways.
  • Evaluated the impact of S779 signaling on cell survival and proliferation in Ba/F3 cells and BALB/c 3T3 fibroblasts.

Main Results:

  • FGFR2 is phosphorylated on S779 in response to FGF2.
  • Phosphorylated S779 serves as a docking site for 14-3-3 proteins.
  • S779 signaling is crucial for full activation of phosphatidylinositol 3-kinase and Ras/MAPK pathways.
  • S779 signaling is essential for promoting cell survival and proliferation.

Conclusions:

  • A new mode of FGFR2 signaling via phosphoserine (S779) and 14-3-3 proteins regulates intracellular pathways.
  • This mechanism expands the signaling repertoire for FGFR2, contributing to pleiotropic biological responses.
  • Conserved phosphoserine motifs in other cell surface receptors suggest broader functional implications.

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