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Activated SRC oncogene phosphorylates R-ras and suppresses integrin activity.

June X Zou1, Yanqiu Liu, Elena B Pasquale

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

The Journal of Biological Chemistry
|October 30, 2001
PubMed
Summary

Src kinase reduces cell adhesion by phosphorylating R-Ras, a key regulator of integrin activity. This molecular mechanism explains how Src-transformed cells exhibit decreased adhesion and increased invasiveness.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Src kinase is known to decrease cell adhesion.
  • R-Ras, a small GTPase, maintains cell adhesion via integrin activity.
  • Eph receptor kinases can regulate R-Ras activity through phosphorylation.

Purpose of the Study:

  • To investigate the mechanism by which Src regulates cell adhesion.
  • To determine if Src-mediated regulation of cell adhesion involves R-Ras and integrins.

Main Methods:

  • Transfection of 293T cells with activated Src (v-Src).
  • In vitro kinase assays using v-Src and R-Ras.
  • Co-immunoprecipitation studies with R-Ras and Src.
  • Site-directed mutagenesis of R-Ras phosphorylation site (tyrosine 66).

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Main Results:

  • Activated Src (v-Src and Src527) phosphorylates R-Ras.
  • Src and R-Ras co-immunoprecipitated, indicating a complex formation.
  • Phosphorylation of R-Ras by Src occurs at tyrosine 66, critical for integrin activity.
  • Mutating tyrosine 66 of R-Ras confers partial resistance to Src-induced cell adhesion reduction.

Conclusions:

  • Src kinase directly phosphorylates R-Ras at tyrosine 66.
  • This phosphorylation event by Src impairs R-Ras function in maintaining integrin activity.
  • Src-mediated regulation of R-Ras contributes to reduced cell adhesion and increased invasiveness in Src-transformed cells.