Ezrin/radixin/moesin: versatile controllers of signaling molecules and of the cortical cytoskeleton

Int J Biochem Cell Biol. 2008;40(3):344-9. doi: 10.1016/j.biocel.2007.02.012. Epub 2007 Feb 22.


Ezrin, radixin and moesin (ERM) proteins are widely distributed proteins located in the cellular cortex, in microvilli and adherens junctions. They feature an N-terminal membrane binding domain linked by an alpha-helical domain to the C-terminal actin-binding domain. In the dormant state, binding sites in the N-terminal domain are masked by interactions with the C-terminal region. The alpha-helical domain also contributes to masking of binding sites. A specific sequence of signaling events results in dissociation of these intramolecular interactions resulting in ERM activation. ERM molecules have been implicated in mediating actin-membrane linkage and in regulating signaling molecules. They are involved in cell membrane organization, cell migration, phagocytosis and apoptosis, and may also play cell-specific roles in tumor progression. Their precise involvement in these processes has yet to be elucidated.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / metabolism
  • Adherens Junctions / physiology
  • Animals
  • Cytoskeletal Proteins / chemistry
  • Cytoskeletal Proteins / physiology*
  • Cytoskeleton / physiology*
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / physiology*
  • Microfilament Proteins / chemistry
  • Microfilament Proteins / physiology*
  • Microvilli / physiology
  • Protein Conformation


  • Actins
  • Cytoskeletal Proteins
  • Membrane Proteins
  • Microfilament Proteins
  • ezrin
  • moesin
  • radixin