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FAK was originally isolated as a substrate of the protein tyrosine kinase Src and was subsequently shown to be a Src-binding protein. FAK plays a very important role in integrin-mediated signaling and in modulating such processes as cell growth, differentiation, wound healing, and tumor metastasis. Although the precise function of FAK is currently undefined, some recent observations strongly indicate that FAK may suppress apoptosis in certain cancer cells. For this reason, FAK has been considered as a target for anticancer therapy. We have chosen to study the focal adhesion target (FAT) domain of FAK. Mutation studies have shown that this domain was responsible for localization of FAK to focal adhesions. A truncated isoform of FAK, which is identical to the C-terminal portion of full-length FAK and includes the Fat domain, inhibits cell spreading and migration. The structural studies of the FAT domain should provide detailed information about the physical and functional interactions between FAK and other adhesion molecules.