Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

MSN (Moesin)

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

Synonyms

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...
This is a preview of subscription content, log in to check access.

References

  1. Amar S, Oyaisu K, Li L, Van Dyke T. Moesin: a potential LPS receptor on human monocytes. J Endotoxin Res. 2001;7:281–6. doi:10.1177/09680519010070041001.CrossRefPubMedGoogle Scholar
  2. Amieva MR, Furthmayr H. Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts. Exp Cell Res. 1995;219:180–96. doi:10.1006/excr.1995.1218.CrossRefPubMedGoogle Scholar
  3. Barrero-Villar M, Cabrero JR, Gordon-Alonso M, Barroso-Gonzalez J, Alvarez-Losada S, Munoz-Fernandez MA, Sanchez-Madrid F, Valenzuela-Fernandez A. Moesin is required for HIV-1-induced CD4-CXCR4 interaction, F-actin redistribution, membrane fusion and viral infection in lymphocytes. J Cell Sci. 2009;122:103–13.CrossRefPubMedGoogle Scholar
  4. Ben-Aissa K, Patino-Lopez G, Belkina NV, Maniti O, Rosales T, Hao J-J, Kruhlak MJ, Knutson JR, Picart C, Shaw S. Activation of moesin, a protein that links actin cytoskeleton to the plasma membrane, occurs by phosphatidylinositol 4,5-bisphosphate (PIP2) binding sequentially to two sites and releasing an autoinhibitory linker. J Biol Chem. 2012;287:16311–23. doi:10.1074/jbc.M111.304881.CrossRefPubMedPubMedCentralGoogle Scholar
  5. DeWitt JJ, Grepo N, Wilkinson B, Evgrafov OV, Knowles JA, Campbell DB. Impact of the autism-associated long noncoding RNA MSNP1AS on neuronal architecture and gene expression in human neural progenitor cells. Genes. 2016;7:76. doi:10.3390/genes7100076.CrossRefPubMedCentralGoogle Scholar
  6. Estecha A, Sanchez-Martin L, Puig-Kroger A, Bartolome RA, Teixido J, Samaniego R, Sanchez-Mateos P. Moesin orchestrates cortical polarity of melanoma tumour cells to initiate 3D invasion. J Cell Sci. 2009;122:3492–501. doi:10.1242/jcs.053157.CrossRefPubMedGoogle Scholar
  7. Ilani T, Khanna C, Zhou M, Veenstra TD, Bretscher A. Immune synapse formation requires ZAP-70 recruitment by ezrin and CD43 removal by moesin. J Cell Biol. 2007;179:733–46. doi:10.1083/jcb.200707199.CrossRefPubMedPubMedCentralGoogle Scholar
  8. Kerin T, Ramanathan A, Rivas K, Coetzee GA, Campbell DB. A noncoding RNA antisense to moesin at 5p14.1 in autism. Sci Transl Med. 2012;128:128ra40. doi:10.1126/scitranslmed.3003479.CrossRefGoogle Scholar
  9. Kubo Y, Yoshii H, Kamiyama H, Tominaga C, Tanaka Y, Sato H, Yamamoto N. Ezrin, Radixin, and Moesin (ERM) proteins function as pleiotropic regulators of human immunodeficiency virus type 1 infection. Virology. 2008;375:130–40. doi:10.1016/j.virol.2008.01.047.CrossRefPubMedGoogle Scholar
  10. Lankes WT, Furthmayr H. Moesin: a member of the protein 4.1-talin-ezrin family of proteins. Proc Natl Acad Sci. 1991;88:8297–301.PubMedPubMedCentralCrossRefGoogle Scholar
  11. Lankes W, Griesmacher A, Grunwald J, Schwartz-Albiez R, Keller R. A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation. Biochem J. 1988;251:831–42. doi:10.1042/bj2510831.CrossRefPubMedPubMedCentralGoogle Scholar
  12. Li Q, Nance MR, Kulikauskas R, Nyberg K, Fehon R, Karplus PA, Bretscher A, Tesmer JJ. Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain. J Mol Biol. 2007;365:1446–59. doi:10.1016/j.jmb.2006.10.075.CrossRefPubMedGoogle Scholar
  13. Liu X, Yang T, Suzuki K, Tsukita S, Ishii M, Zhou S, Wang G, Cao L, Qian F, Taylor S, Oh MJ, Levitan I, Ye RD, Carnegie GK, Zhao Y, Malik AB, Xu J. Moesin and myosin phosphatase confine neutrophil orientation in a chemotactic gradient. J Exp Med. 2015;212:267–80. doi:10.1084/jem.20140508.CrossRefPubMedPubMedCentralGoogle Scholar
  14. Pearson MA, Reczek D, Bretscher A, Karplus PA. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell. 2000;101:259–70. doi:10.1016/S0092-8674(00)80836-3.CrossRefPubMedGoogle Scholar
  15. Polesello C, Delon I, Valenti P, Ferrer P, Payre F. Dmoesin controls actin-based cell shape and polarity during Drosophila melanogaster oogenesis. Nat Cell Biol. 2002;4:782–9. doi:10.1038/ncb856.CrossRefPubMedGoogle Scholar
  16. Shaffer MH, Dupree RS, Zhu P, Saotome I, Schmidt RF, McClatchey AI, Freedman BD, Burkhardt JK. Ezrin and moesin function together to promote T cell activation. J Immunol. 2009;182:1021–32. doi:10.4049/jimmunol.182.2.1021.CrossRefPubMedPubMedCentralGoogle Scholar
  17. Speck O, Hughes SC, Noren NK, Kulikauskas RM, Fehon RG. Moesin functions antagonistically to the Rho pathway to maintain epithelial integrity. Nature. 2003;421(6918):83–7. doi:10.1038/nature01295.CrossRefPubMedGoogle Scholar
  18. Takeuchi K, Sato N, Kasahara H, Funayama N, Nagafuchi A, Yonemura S, Tsukita S, Tsukita S. Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members. J Cell Biol. 1994;125:1371–84. doi:10.1083/jcb.125.6.1371.CrossRefPubMedGoogle Scholar
  19. Wang Q, Fan A, Yuan Y, et al. Role of moesin in advanced glycation end products-induced angiogenesis of human umbilical vein endothelial cells. Sci Report. 2016;6:22749. doi:10.1038/srep22749.CrossRefGoogle Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

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