Focal adhesion kinase regulation by oxidative stress in different cell types

Focal adhesion kinase (FAK) is a tyrosine kinase ubiquitously expressed in cells. It was initially shown to be the initiator of focal adhesion formati on in adherent cells, after its binding to integrins which induce its autop hosphorylation. However, it can be also activated by a great variety of oth er stimuli able to act on different intracellular signaling. Reactive oxyge n species (ROS), which have been shown to act as external or internal cell stimuli, induce tyrosine phosphorylation of FAK, Its autophosphorylation is followed by a submembranous localization which is crucial for many of the biological roles of FAK, including cell spreading, cell migration, cell pro liferation, and prevention of apoptosis, It plays an important role in deve lopment of tumor cells, its regulation could be thus a way of impairing cel l proliferation in cancer, We describe in this review the structure, activi ty, and functions of FAK in different cells and how ROS are able, like othe r stimuli, to induce its phosphorylation and modification of cell morpholog y and structure. The link between ROS and FAK activation could explain the role of ROS in mediating cell proliferation, cell migration, or apoptosis.