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Paradoxical roles of FAK in tumor cell migration and metastasis

Yanhua Zheng1, Zhimin Lu

  • 1Brain Tumor Center and Department of Neuro-Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, USA.

Cell Cycle (Georgetown, Tex.)
|October 16, 2009
PubMed

Insights

Focal adhesion kinase (FAK) typically promotes cell migration, but under certain cancer signaling, it can inhibit it. Activated Ras may drive tumor cell migration by altering FAK phosphorylation and focal adhesion dynamics.

Area of Science:

  • Cell biology
  • Molecular oncology
  • Biochemistry

Background:

  • Focal adhesion kinase (FAK) is a key mediator of integrin signaling, regulating cell survival, proliferation, and migration.
  • FAK is generally considered a positive regulator of normal cell migration and cancer metastasis.
  • Emerging evidence suggests FAK can negatively regulate cancer cell migration under specific oncogenic signaling conditions.

Purpose of the Study:

  • To investigate the dual role of FAK in cancer cell migration.
  • To elucidate the mechanisms by which oncogenic signaling pathways modulate FAK activity and its effect on migration.

Main Methods:

  • Analysis of FAK signaling pathways.
  • Investigating the role of activated Ras and growth factor receptor kinases in FAK regulation.
  • Studying focal adhesion dynamics and turnover at the leading edge of migrating cells.

Main Results:

  • FAK's role in cell migration is context-dependent, influenced by specific oncogenic signaling.
  • Activated Ras can lead to FAK dephosphorylation at Y397.
  • This dephosphorylation facilitates focal adhesion turnover, potentially promoting cancer cell migration.

Conclusions:

  • FAK exhibits a context-specific regulatory role in cancer cell migration.
  • Oncogenic signaling, particularly activated Ras, can reprogram FAK function from a promoter to an inhibitor of migration.
  • Targeting FAK phosphorylation and focal adhesion dynamics may offer novel therapeutic strategies for cancer metastasis.

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