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Vav2 is required for cell spreading.

P A Marignani1, C L Carpenter

  • 1Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, 330 Brookline Avenue, Boston, MA 02215, USA.

The Journal of Cell Biology
|July 13, 2001
PubMed
Summary
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Vav2, a guanine nucleotide exchange factor, regulates Rac activation and cell shape changes. Its activity is dependent on the Src kinase and the pleckstrin homology domain, playing a role in integrin-mediated cell spreading.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Signal Transduction

Background:

  • Vav2 is a Rho family guanine nucleotide exchange factor.
  • The normal function and regulation of Vav2 are not fully understood.
  • Activated Vav2 has transforming potential.

Purpose of the Study:

  • To investigate the pathways regulating Vav2 exchange activity in vivo.
  • To characterize the function of Vav2 in cellular processes.

Main Methods:

  • Overexpression of Vav2 and its mutants (PH and DH domains).
  • Measurement of Rac-GTP levels.
  • Assessment of cell morphology and lamellipodia formation.
  • Use of dominant-negative Src and Src inhibitor PP2.
  • Cell spreading assays on fibronectin.

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Main Results:

  • Vav2 overexpression activates Rac and induces lamellipodia formation.
  • Vav2 nucleotide exchange activity is Src-dependent.
  • The pleckstrin homology (PH) domain is essential for Vav2 exchange activity.
  • Vav2 is not required for growth factor-dependent Rac activation.
  • Vav2 is necessary for integrin-dependent Rac activation and lamellipodia formation in NIH3T3 fibroblasts.

Conclusions:

  • Vav2 is a Src-dependent guanine nucleotide exchange factor for Rac.
  • Vav2 plays a critical role in integrin-mediated cell spreading by regulating Rac activation and lamellipodia formation.
  • Vav2 function is distinct from its role in growth factor signaling pathways.