Integrin-regulated FAK-Src signaling in normal and cancer cells.
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.
Mitra
Satyajit K
SK
The Scripps Research Institute, Department of Immunology, IMM21 10550 N. Torrey Pines Rd, La Jolla, CA 92037, USA.
Schlaepfer
David D
DD
D000818:Animals; D002465:Cell Movement / Q000502:physiology; D002470:Cell Survival; D018450:Disease Progression; D004789:Enzyme Activation; D051416:Focal Adhesion Protein-Tyrosine Kinases / Q000378:metabolism*; D016023:Integrins / Q000378:metabolism*; D009369:Neoplasms / Q000378:metabolism* / Q000473:pathology; D015398:Signal Transduction / Q000502:physiology*; D019061:src-Family Kinases / Q000378:metabolism*
D016023:Integrins; D051416:Focal Adhesion Protein-Tyrosine Kinases; D019061:src-Family Kinases