Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

MSN (Moesin)

  • Katharine A. Michie
  • Sophia C. Goodchild
  • Paul M. G. CurmiEmail author
Reference work entry
DOI: https://doi.org/10.1007/978-3-319-67199-4_101770


Historical Background

Moesin (membrane-organizing extension spike protein) was initially isolated from bovine uterus in 1988. It was first identified as a heparin-binding protein and thought to be extracellular (Lankes et al. 1988), but later shown to be intracellular (Lankes and Furthmayr 1991). Moesin belongs to the ERM family of proteins (ezrin, radixin, and moesin), a subclass of the large protein 4.1 superfamily that also includes protein 4.1, talin and merlin. The ERM family of proteins is credited with coupling filamentous actin to the cell membrane and has roles in numerous cellular processes involving modification of the cortical actin network in conjunction with the plasma membrane.

Distribution and Cell Biology

Early in metazoan evolution, a single ERM protein and a single, related merlin protein arose (see Fig. 1). Only a single ERM protein is found in invertebrates...
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Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  • Katharine A. Michie
    • 1
  • Sophia C. Goodchild
    • 1
  • Paul M. G. Curmi
    • 1
    Email author
  1. 1.School of PhysicsUniversity of New South WalesSydneyAustralia