The FERM domain: organizing the structure and function of FAK.
Focal adhesion kinase (FAK) is a scaffold and tyrosine kinase protein that binds to itself and cellular partners through its four-point-one, ezrin, radixin, moesin (FERM) domain. Recent structural work reveals that regulatory protein partners convert auto-inhibited FAK into its active state by binding to its FERM domain. Further, the identity of FAK FERM domain-interacting proteins yields clues as to how FAK coordinates diverse cellular responses, including cell adhesion, polarization, migration, survival and death, and suggests that FERM domains might mediate information transfer between the cell cortex and nucleus. Importantly, the FAK FERM domain might act as a paradigm for the actions of other FERM domain-containing proteins.
Edinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, Western General Hospital, Crewe Road South, Edinburgh EH4 2XR, UK. M.Frame@ed.ac.uk
Margaret C
MC
Frame
Hitesh
H
Patel
Bryan
B
Serrels
Daniel
D
Lietha
Michael J
MJ
Eck
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D002468:Cell Physiological Phenomena; D003593:Cytoplasm / Q000378:metabolism; D051416:Focal Adhesion Protein-Tyrosine Kinases / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
D051416:Focal Adhesion Protein-Tyrosine Kinases