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The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization

Silvia Continolo1, Anna Baruzzi, Meytham Majeed

  • 1Department of Pathology, Section of General Pathology, University of Verona, Verona, Italy.

Experimental Cell Research
|November 25, 2004
PubMed

Insights

The proto-oncogene Fgr regulates myeloid leukocyte migration by impacting integrin signaling. Membrane-bound Fgr enhances cell migration through FAK/Pyk2 pathways, activating Rac and p190RhoGAP.

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Fgr is a proto-oncogene tyrosine kinase involved in integrin signaling.
  • Myeloid leukocytes utilize Fgr for regulating cell migration.

Purpose of the Study:

  • To investigate the role of specific Fgr domains in regulating myeloid leukocyte cell migration.
  • To elucidate the molecular mechanisms by which Fgr influences cell migration.

Main Methods:

  • Expression of various Fgr molecules in COS-7 cells.
  • Analysis of cell migration on fibronectin.
  • Assessment of protein phosphorylation (PI3K, cortactin, FAK, Vav2, p190RhoGAP).
  • Investigation of protein-protein interactions (Fgr, FAK, p190RhoGAP, Pyk2).

Main Results:

  • Full-length, membrane-bound Fgr significantly increased cell migration and enhanced phosphorylation of PI3K, cortactin, and FAK.
  • Fgr promoted Rac GTP loading and Vav2 phosphorylation, and its interaction with the FAK/p190RhoGAP complex was membrane-dependent.
  • A kinase-defective Fgr mutant showed reduced but significant cell migration, Rac activation, and complex formation with p190RhoGAP/FAK.

Conclusions:

  • Proto-oncogene Fgr regulates cell migration through a pathway involving FAK/Pyk2.
  • Fgr activation of Rac and the Rho inhibitor p190RhoGAP is crucial for cell migration.
  • Membrane localization of Fgr is essential for its function in regulating cell migration.

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