GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
TableEdit
PMID:16919435
You don't have sufficient rights on this wiki to edit tables. Perhaps you need to log in. Changes you make in the Table editor will not be saved back to the wiki
See Help for Help on this wiki. See the documentation for how to use the table editor
Citation |
Mitra, SK and Schlaepfer, DD (2006) Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr. Opin. Cell Biol. 18:516-23 |
---|---|
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. |
Links |
PubMed Online version:10.1016/j.ceb.2006.08.011 |
Keywords |
Animals; Cell Movement/physiology; Cell Survival; Disease Progression; Enzyme Activation; Focal Adhesion Protein-Tyrosine Kinases/metabolism; Integrins/metabolism; Neoplasms/metabolism; Neoplasms/pathology; Signal Transduction/physiology; src-Family Kinases/metabolism |
public |
Cancel |