Blog
About

36
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      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

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          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.

          Related collections

          Author and article information

          Journal
          10.1016/j.ceb.2006.08.011
          16919435

          Comments

          Comment on this article