ABSTRACT
Cellular adhesion to the extracellular matrix is a critical regulator of fundamental processes including growth, differentiation, death, and migration. The ability of focal adhesions to organize a competent signal transducing complex is suggested by the observed interaction of heterodimeric transmembrane integrin receptors with focal adhesion associated tyrosine phosphorylated proteins. Among the proteins phosphorylated as a result of integrin clustering is a protein tyrosine kinase found within the focal adhesion. The chapter reviews methodology used to identify focal adhesion kinase (FAK) binding proteins. It discusses the identification of in vivo and in vitro protein interactions, as well as methods for detecting co-localization of FAK and its binding partners in intact cells using immunofluorescence. Transmission of signals from extracellular cues to intracellular compartments involves protein phosphorylation necessitating protein-protein interactions.
