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Related Experiment Videos

An Eph receptor regulates integrin activity through R-Ras.

J X Zou1, B Wang, M S Kalo

  • 1Cancer Research Center, The Burnham Institute, La Jolla, CA 92037, USA.

Proceedings of the National Academy of Sciences of the United States of America
|November 26, 1999
PubMed
Summary

Eph receptor tyrosine kinase EphB2 controls cell adhesion by regulating the small GTPase R-Ras. This pathway, involving R-Ras phosphorylation, reduces cell binding and may impact tumor invasion and blood vessel growth.

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Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Integrins mediate cell adhesion to extracellular matrices and blood proteins, crucial for processes like platelet aggregation and leukocyte extravasation.
  • R-Ras, a small intracellular GTPase, regulates integrin ligand-binding activity from inside the cell.
  • Altered cell adhesion is implicated in tumor cell invasion.

Purpose of the Study:

  • To investigate the role of Eph receptor tyrosine kinases in regulating integrin activity.
  • To elucidate the mechanism by which EphB2 controls cell adhesion via R-Ras.

Main Methods:

  • Activation of EphB2 in cells.
  • Analysis of cell adhesion to integrin ligands.
  • Phosphorylation site mapping of R-Ras.

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  • Expression of R-Ras variants resistant to phosphorylation.

    • Main Results:

    • EphB2 activation leads to decreased cell adhesion to integrin ligands.
    • A specific tyrosine residue in the R-Ras effector domain is phosphorylated upon EphB2 activation.
    • Phosphorylation of R-Ras is causally linked to the anti-adhesive effect of EphB2.
    • A phosphorylation-resistant R-Ras variant abrogates EphB2-mediated loss of cell adhesion.

    Conclusions:

    • EphB2 regulates integrin-mediated cell adhesion through a novel pathway involving R-Ras phosphorylation.
    • This Eph/R-Ras pathway provides a molecular mechanism for Eph receptor-mediated repulsion in axonal pathfinding.
    • The pathway may contribute to tumor cell invasion and angiogenesis by reducing cell adhesiveness.