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Encyclopedia of Signaling Molecules pp 3232–3238Cite as

MSN (Moesin)

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Synonyms

Epididymis luminal protein 70; HEL70; Membrane-organizing extension spike protein; Moesin; MSN

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 such...

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References

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Authors and Affiliations

  1. School of Physics, University of New South Wales, Sydney, NSW, 2052, Australia

    Katharine A. Michie, Sophia C. Goodchild & Paul M. G. Curmi

Authors
  1. Katharine A. Michie
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  2. Sophia C. Goodchild
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  3. Paul M. G. Curmi
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Corresponding author

Correspondence to Paul M. G. Curmi .

Editor information

Editors and Affiliations

  1. Department of Molecular Science and Technology, Ajou University, Suwon, Korea

    Sangdun Choi

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Michie, K.A., Goodchild, S.C., Curmi, P.M.G. (2018). MSN (Moesin). In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101770

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