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Regulation of Ras and Rho small G proteins by SHP-2.

A Kodama1, T Matozaki, M Shinohara

  • 1Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Japan.

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
|October 31, 2001
PubMed
Summary

SHP-2 (a protein tyrosine phosphatase) promotes cell scattering induced by hepatocyte growth factor/scatter factor (HGF/SF). SHP-2-DA enhances HGF/SF-induced scattering by modulating Ras and Rho signaling pathways.

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Area of Science:

  • Cell biology
  • Molecular signaling
  • Cancer research

Background:

  • Hepatocyte growth factor/scatter factor (HGF/SF) signaling via c-Met receptor drives cell scattering.
  • SHP-2, a protein tyrosine phosphatase, positively regulates HGF/SF-induced cell scattering by modulating Rho activity.
  • Previous studies established SHP-2's role in stress fiber and focal adhesion formation.

Purpose of the Study:

  • To investigate the role of a dominant active mutant of SHP-2 (SHP-2-DA) in HGF/SF-induced cell scattering.
  • To elucidate the downstream signaling pathways regulated by SHP-2-DA in this process.

Main Methods:

  • Expression of SHP-2-DA in MDCK cells.
  • Analysis of cell morphology, lamellipodia formation, and E-cadherin/beta-catenin localization.

Related Experiment Videos

  • Assessment of MAP kinase activation.
  • Inhibition of MEK pathway.
  • Expression of dominant-active Rho or Vav2 mutants.

    • Main Results:

    • SHP-2-DA expression increased lamellipodia formation and ruffling.
    • SHP-2-DA decreased E-cadherin and beta-catenin at cell-cell adhesion sites.
    • SHP-2-DA enhanced HGF/SF-induced cell scattering and activated MAP kinase independently of HGF/SF.
    • MEK inhibition, dominant-active Rho, or Vav2 expression reversed SHP-2-DA-induced phenotypes.

    Conclusions:

    • SHP-2 plays a critical role in HGF/SF-induced cell scattering.
    • SHP-2 regulates cell scattering through distinct pathways involving Ras and Rho small G proteins.