Focal adhesion kinase (FAK) is a cytoplasmic tyrosine kinase that plays critical roles in integrin-mediated signal transductions and also participates in signaling by other cell surface receptors. In integrin-mediated cell adhesion, FAK is activated via disruption of an auto-inhibitory intra-molecular interaction between its amino terminal FERM domain and the central kinase domain.


Focal adhesion kinase (FAK) is a ubiquitously expressed multidomain protein tyrosine kinase that has been shown to regulate cell adhesion, migration, proliferation, and survival. It was discovered in 1992 as a highly tyrosine-phosphorylated protein tyrosine kinase that localizes to focal adhesions. FAK is expressed in most tissues and is highly conserved across species. Due to the inherent characteristics of FAK both as a kinase and as a scaffold protein, FAK is involved in numerous signaling cascades, and contributes to the pathology of a number of diseases. FAK has been linked to the regulation of (EGF) and the

Due to its role in cell migration, cell cycle progression, and apoptosis, it is not surprising that several lines of evidence have linked FAK to cancer. FAK is overexpressed in several types of cancer including thyroid, prostate, cervix, colon, rectum, oral epithelium, and ovarian, and increased FAK levels are often associated with malignancy and metastasis. While FAK has been implicated in various processes necessary for metastasis and invasion, its precise role in malignancy is unclear. First, FAK has been implicated in the release of matrix metallo-proteinases, which degrade the basement membrane allowing cells to enter the bloodstream and invade other tissues. Furthermore, FAK is linked to the release of vascular endothelial growth factor (VEGF), which controls the growth of new blood vessels necessary for growing tumors.

Because of the importance of FAK in cell migration and its connection to invasive, metastatic cancer, inhibition of FAK has become an attractive strategy for treating cancer. Inhibition of FAK expression by antisense RNA reduces cell migration and invasion and increases cell death in carcinoma and melanoma cells. Furthermore, inhibition of FAK by siRNA in lung cancer cells decreased migration and the ability to grow in soft agar. These data suggest that FAK could be a therapeutic target for treating cancer.


Cable, Jennifer Lynn.Investigation of Phosphorylation and Ligand Binding of the Focal Adhesion Targeting Domain of Focal Adhesion Kinase. The University of North Carolina at Chapel Hill, 2011.

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