Multiple connections link FAK to cell motility and invasion.
The ability of intracellular signaling networks to orchestrate a complex biological response such as cell motility requires that individual signaling proteins must act as integrators, responding to multiple extracellular inputs and regulating multiple signaling pathway outputs. In this review, we highlight recent findings that place focal adhesion kinase (FAK) in an important receptor-proximal position in the regulation of growth factor and integrin-stimulated cell motility. Emphasis is placed on the molecular mechanisms of FAK activation, connections of FAK to focal contact formation as well as turnover, and the potential that FAK function in promoting cell invasion may be distinct from its role in cell motility.
Schlaepfer
David D
DD
The Scripps Research Institute, Department of Immunology, IMM26, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA. dschlaep@scripps.edu
Mitra
Satyajit K
SK
D002465:Cell Movement / Q000502:physiology*; D004789:Enzyme Activation; D005347:Fibroblasts / Q000502:physiology; D051416:Focal Adhesion Protein-Tyrosine Kinases; D016023:Integrins / Q000502:physiology; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000502:physiology*; D015398:Signal Transduction
D016023:Integrins; D011505:Protein-Tyrosine Kinases; D051416:Focal Adhesion Protein-Tyrosine Kinases