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Related Experiment Videos

Ligand-induced transphosphorylation between different FGF receptors.

F Bellot1, G Crumley, J M Kaplow

  • 1Molecular Biology Department, Rhône-Poulenc Rorer Central Research, King of Prussia, PA 19406.

The EMBO Journal
|October 1, 1991
PubMed
Summary

Fibroblast growth factor receptors (FGFR) undergo transphosphorylation, where a kinase-negative FGFR mutant is activated by a co-expressed active FGFR. This mechanism, involving both homologous and heterologous receptor interactions, is crucial for cell signaling.

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Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Receptor Tyrosine Kinases

Background:

  • Fibroblast growth factors (FGFs) bind to fibroblast growth factor receptors (FGFRs) with high affinity.
  • FGFR tyrosine autophosphorylation is critical for downstream signaling.
  • The precise mechanism of FGFR autophosphorylation, especially in co-expression systems, requires further elucidation.

Purpose of the Study:

  • To investigate the mechanism of fibroblast growth factor receptor (FGFR) tyrosine autophosphorylation.
  • To determine if kinase-negative FGFR mutants can be phosphorylated by co-expressed active FGFRs.
  • To explore homologous and heterologous transphosphorylation between FGFRs in living cells.

Main Methods:

  • Generation of NIH 3T3 cell lines co-expressing different combinations of wild-type and kinase-negative FGFR mutants (bek and flg).

Related Experiment Videos

  • Immunoprecipitation using FGFR-specific antisera to confirm receptor expression.
  • Stimulation with acidic FGF (aFGF) followed by immunoprecipitation and immunoblotting with anti-phosphotyrosine antibodies to detect phosphorylation.

    • Main Results:

    • Co-expression of active and kinase-negative FGFR mutants was confirmed in transfected NIH 3T3 cells.
    • Acidic FGF stimulation induced tyrosine phosphorylation of kinase-negative FGFR mutants in all tested cell lines.
    • Both homologous (bek-bek, flg-flg) and heterologous (bek-flg, flg-bek) transphosphorylation of FGFRs were observed in living cells.

    Conclusions:

    • Tyrosine autophosphorylation of kinase-negative FGFR mutants occurs via a transphosphorylation mechanism.
    • Heterologous transphosphorylation between different FGFRs (bek and flg) happens in living cells.
    • Heterologous transphosphorylation may amplify cellular responses to various FGFs and their receptors.