Regulation of cortical structure by the ezrin-radixin-moesin protein family

Curr Opin Cell Biol. 1999 Feb;11(1):109-16. doi: 10.1016/s0955-0674(99)80013-1.


Molecules involved in ERM (ezrin-radixin-moesin) based attachment of membrane proteins to the cortical cytoskeleton in cell surface structures have been identified. In lymphocytes, a direct interaction is seen with extracellular matrix receptors and intercellular adhesion molecules. In polarized epithelial cells, an adaptor molecule named EBP50 provides a bridge between the amino-terminal domain of ezrin and the cytoplasmic regions of plasma membrane proteins, including the cystic fibrosis transmembrane conductance regulator (CFTR) and the beta2 adrenergic receptor. ERM proteins are conformationally regulated - binding sites for EBP50 and F actin are masked in the dormant molecules and activation leads to exposure of these sites. The mechanism of activation, however, remains to be fully elucidated. ERM proteins also play a role in the Rho and Rac signaling pathways: activated ERM proteins can dissociate Rho-GDI (GDP dissociation inhibitor) from Rho and thereby activate Rho-dependent pathways.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Blood Proteins / chemistry
  • Blood Proteins / metabolism*
  • Cells, Cultured
  • Cytoskeletal Proteins*
  • Cytoskeleton / metabolism*
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Microfilament Proteins / chemistry
  • Microfilament Proteins / metabolism*
  • Models, Biological
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism*
  • Protein Conformation
  • Signal Transduction


  • Blood Proteins
  • Cytoskeletal Proteins
  • Membrane Proteins
  • Microfilament Proteins
  • Phosphoproteins
  • ezrin
  • moesin
  • radixin