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Integrin-regulated FAK-Src signaling in normal and cancer cells.

Current Opinion in Cell Biology

metabolism, src-Family Kinases, physiology, Signal Transduction, pathology, Neoplasms, Integrins, Focal Adhesion Protein-Tyrosine Kinases, Enzyme Activation, Disease Progression, Cell Survival, Cell Movement, Animals

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      Abstract

      Integrins can alter cellular behavior through the recruitment and activation of signaling proteins such as non-receptor tyrosine kinases including focal adhesion kinase (FAK) and c-Src that form a dual kinase complex. The FAK-Src complex binds to and can phosphorylate various adaptor proteins such as p130Cas and paxillin. In normal cells, multiple integrin-regulated linkages exist to activate FAK or Src. Activated FAK-Src functions to promote cell motility, cell cycle progression and cell survival. Recent studies have found that the FAK-Src complex is activated in many tumor cells and generates signals leading to tumor growth and metastasis. As both FAK and Src catalytic activities are important in promoting VEGF-associated tumor angiogenesis and protease-associated tumor metastasis, support is growing that FAK and Src may be therapeutically relevant targets in the inhibition of tumor progression.

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      Journal
      10.1016/j.ceb.2006.08.011
      16919435

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