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Fibroblast growth factor-2 interacts with free ribosomal protein S19

F Soulet1, T Al Saati, S Roga

  • 1Laboratoire de Biologie Vasculaire, IPBS/CNRS, 205 Rte de Narbonne, 31077 Toulouse Cedex, France.

Biochemical and Biophysical Research Communications
|November 22, 2001
PubMed

Insights

Fibroblast Growth Factor 2 (FGF-2) enters cells and interacts with RPS19, a ribosomal protein. This study reveals FGF-2 binds to free RPS19 in vivo, suggesting a novel cellular signaling role.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Interactions

Background:

  • Fibroblast Growth Factor 2 (FGF-2) is internalized by cells and can translocate to the nucleus.
  • Understanding the FGF-2 signaling pathway requires identifying interacting cytoplasmic proteins.

Purpose of the Study:

  • To identify proteins associated with FGF-2 in the cytoplasm.
  • To investigate the interaction between FGF-2 and RPS19.

Main Methods:

  • GST-FGF-2 pull-down assays to isolate FGF-2-associated cytoplasmic proteins.
  • In vitro binding assays to confirm direct interaction between FGF-2 and RPS19.
  • Co-immunoprecipitation from FGF-2-stimulated cell extracts to detect in vivo interactions.

Main Results:

  • RPS19, a component of the 40S small ribosomal subunit, was identified as an FGF-2-interacting protein.
  • FGF-2 directly interacts with RPS19 in vitro.
  • FGF-2 co-immunoprecipitated with RPS19 from cell extracts, indicating an in vivo interaction with free RPS19.

Conclusions:

  • A pool of free RPS19 exists in the cytoplasm, independent of the 40S ribosomal subunit.
  • FGF-2 interacts with this free pool of RPS19 in vivo.
  • These findings suggest a potential novel role for FGF-2 in cellular signaling pathways involving free RPS19.

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