The FERM domain: organizing the structure and function of FAK

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

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Nucleus / metabolism
  • Cell Physiological Phenomena
  • Cytoplasm / metabolism
  • Focal Adhesion Protein-Tyrosine Kinases / chemistry*
  • Focal Adhesion Protein-Tyrosine Kinases / metabolism*
  • Humans
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Tertiary*
  • Signal Transduction*

Substances

  • Focal Adhesion Protein-Tyrosine Kinases