FAK (Focal Adhesion Kinase, or PTK2) is a protein tyrosine kinase that is not associated with receptors and is not located on membranes. It is activated at the sites of integrin clustering and cell-matrix adhesions by autophosphorylation (at Tyr397), Src, and other tyrosine kinases. By transferring signals governing cell migration, adhesion, and survival from the extracellular matrix to the cytoplasm, FAK mediates integrin-based cell signaling.
Many tumors, including those from the head and neck, colon, breast, prostate, liver, and thyroid, overexpress FAK. Additionally, in these tumors, FAK overexpression is strongly associated with an invasive phenotype. Glioblastomas and ovarian cancer cells are less likely to invade when dominant-negative FAK fragments are overexpressed and FAK signaling is inhibited. FAK is a crucial target for the creation of anti-metastatic and anti-neoplastic medications.
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