Activation of integrins in the extracellular matrix (ECM) of eukaryotic cells promotes the formation of membrane adhesion complexes, known as focal adhesions, which can include cytoskeletal proteins and protein tyrosine kinases, such as focal adhesion kinase (FAK). Phosphorylation events occurring within focal adhesions influence numerous processes that include mitogenic signaling, cell survival, and cell motility. FAK is a non-receptor tyrosine kinase that is ubiquitously expressed and highly conserved between species. FAK is recruited by Integrin clusters and variably phosphorylated depending on the effector molecules present in the focal adhesion. Phosphorylation of FAK Tyr 397 decreases during serum starvation, contact inhibition, and cell cycle arrest, all conditions under which activating FAK Tyr 407 phosphorylation increases.