ERM proteins: from cellular architecture to cell signaling

Biol Cell. 2000 Aug;92(5):305-16. doi: 10.1016/s0248-4900(00)01078-9.


ERM (ezrin/radixin/moesin) proteins, concentrated in actin rich cell-surface structures, cross-link actin filaments with the plasma membrane. They are involved in the formation of microvilli, cell-cell adhesion, maintenance of cell shape, cell motility and membrane trafficking. Recent analyses reveal that they are not only involved in cytoskeleton organization but also in signaling pathway. They play an important role in the activation of members of the Rho family by recruiting their regulators. The functions of ERM proteins are regulated by their conformational charges: the intramolecular interaction between the N- and C-terminal domains of ERM proteins charges masks several binding sites, leading to a dormant protein. Different activation signals regulate ERM proteins functions by modulating these intramolecular interactions. The involvement of ERM proteins in many signaling pathways has led to study their role during development of different species.

Publication types

  • Review

MeSH terms

  • Actins / metabolism
  • Animals
  • Blood Proteins / chemistry
  • Blood Proteins / metabolism*
  • Cell Adhesion
  • Cell Membrane / metabolism
  • Cell Movement
  • Cytoskeletal Proteins / chemistry
  • Cytoskeletal Proteins / metabolism*
  • Cytoskeleton / metabolism*
  • Embryonic and Fetal Development
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Microfilament Proteins / chemistry
  • Microfilament Proteins / metabolism*
  • Neuropeptides*
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism*
  • Signal Transduction*


  • Actins
  • Blood Proteins
  • Cytoskeletal Proteins
  • Membrane Proteins
  • Microfilament Proteins
  • Neuropeptides
  • Phosphoproteins
  • erythrocyte membrane band 4.1 protein
  • erythrocyte membrane protein band 4.1-like 1
  • ezrin
  • moesin
  • radixin