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Nat Rev Mol Cell Biol. 2010 Nov;11(11):802-14. doi: 10.1038/nrm2996.

The FERM domain: organizing the structure and function of FAK.

Author information

1
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

Abstract

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.

PMID:
20966971
DOI:
10.1038/nrm2996
[Indexed for MEDLINE]

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