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Exogenously added fibroblast growth factor 2 (FGF-2) to NIH3T3 cells interacts with nuclear ribosomal S6 kinase 2

Fabienne Soulet1, Karine Bailly, Stéphane Roga

  • 1Laboratoire de Biologie Vasculaire, Institut de Pharmacologie et de Biologie Structurale, Unité Mixte de Recherche 5089, 205 Route de Narbonne, 31077 Toulouse, France.

The Journal of Biological Chemistry
|May 10, 2005
PubMed

Insights

Fibroblast growth factor 2 (FGF-2) enters cell nuclei and interacts with ribosomal S6 kinase 2 (RSK2). This interaction sustains RSK2 activity during the cell cycle, crucial for cell growth.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Fibroblast growth factor 2 (FGF-2) is found in cell nuclei across various tissues.
  • The nuclear activity and function of FGF-2 are not fully understood.

Purpose of the Study:

  • To investigate the interaction between FGF-2 and nuclear ribosomal S6 kinase 2 (RSK2).
  • To determine the role of this interaction in RSK2 activation and cell cycle progression.

Main Methods:

  • Exogenous application of FGF-2 to NIH3T3 cells.
  • In vitro studies using purified proteins to map interaction domains.
  • Analysis of FGF-2 mutants for RSK2 interaction and activity.

Main Results:

  • Exogenous FGF-2 enters NIH3T3 cell nuclei and interacts with active RSK2.
  • FGF-2 directly binds to specific domains within both the NH2-terminal and COOH-terminal kinase domains of RSK2.
  • This interaction is essential for maintaining sustained RSK2 activation during the G1 phase of the cell cycle.

Conclusions:

  • FGF-2 directly interacts with RSK2, modulating its activity in a cell cycle-dependent manner.
  • The interaction between FGF-2 and RSK2 is critical for sustained RSK2 activation in G1 phase.
  • Specific amino acid residues in FGF-2 mediate its interaction with RSK2, impacting RSK2 activity in vivo.

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