Moesin Explained

Moesin is a protein that in humans is encoded by the MSN gene.^{[1] [2]}

Moesin (for membrane-organizing extension spike protein) is a member of the ERM protein family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons.

Moesin is localized to filopodia and other membranous protrusions that are important for cell–cell recognition and signaling and for cell movement.^[3]

Moesin has FERM domain at N-terminal.

Interactions

Moesin has been shown to interact with:

• CD43^{[4] [5]}
• ICAM3^{[6] [7]}
• Neutrophil cytosolic factor 1,^[8]
• Neutrophil cytosolic factor 4^[8]
• VCAM-1^[9]
• EZR^{[10] [11] [12]}

Further reading

• Tsukita S, Yonemura S . ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction . Curr. Opin. Cell Biol. . 9 . 1 . 70–5 . 1997 . 9013673 . 10.1016/S0955-0674(97)80154-8 .
• Vaheri A, Carpén O, Heiska L, Helander TS, Jääskeläinen J, Majander-Nordenswan P, Sainio M, Timonen T, Turunen O . The ezrin protein family: membrane-cytoskeleton interactions and disease associations . Curr. Opin. Cell Biol. . 9 . 5 . 659–66 . 1997 . 9330869 . 10.1016/S0955-0674(97)80119-6 .
• Matarrese P, Malorni W . Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death . Cell Death Differ. . 12 . 932–41 . 2005 . Suppl 1 . 15818415 . 10.1038/sj.cdd.4401582 . free .
• Gary R, Bretscher A . Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site . Mol. Biol. Cell . 6 . 8 . 1061–75 . 1995 . 7579708 . 301263 . 10.1091/mbc.6.8.1061 .
• Schwartz-Albiez R, Merling A, Spring H, Möller P, Koretz K . Differential expression of the microspike-associated protein moesin in human tissues . Eur. J. Cell Biol. . 67 . 3 . 189–98 . 1995 . 7588875 .
• Schneider-Schaulies J, Dunster LM, Schwartz-Albiez R, Krohne G, ter Meulen V . Physical association of moesin and CD46 as a receptor complex for measles virus . J. Virol. . 69 . 4 . 2248–56 . 1995 . 7884872 . 188894 . 10.1128/JVI.69.4.2248-2256.1995.
• Wilgenbus KK, Hsieh CL, Lankes WT, Milatovich A, Francke U, Furthmayr H . Structure and localization on the X chromosome of the gene coding for the human filopodial protein moesin (MSN) . Genomics . 19 . 2 . 326–33 . 1994 . 8188263 . 10.1006/geno.1994.1065 . free .
• Gary R, Bretscher A . Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins . Proc. Natl. Acad. Sci. U.S.A. . 90 . 22 . 10846–50 . 1993 . 8248180 . 47875 . 10.1073/pnas.90.22.10846 . 1993PNAS...9010846G . free .
• Dunster LM, Schneider-Schaulies J, Löffler S, Lankes W, Schwartz-Albiez R, Lottspeich F, ter Meulen V . Moesin: a cell membrane protein linked with susceptibility to measles virus infection . Virology . 198 . 1 . 265–74 . 1994 . 8259662 . 10.1006/viro.1994.1029 .
• Nakamura F, Amieva MR, Furthmayr H . Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets . J. Biol. Chem. . 270 . 52 . 31377–85 . 1995 . 8537411 . 10.1074/jbc.270.52.31377 . free .
• Ott DE, Coren LV, Kane BP, Busch LK, Johnson DG, Sowder RC, Chertova EN, Arthur LO, Henderson LE . Cytoskeletal proteins inside human immunodeficiency virus type 1 virions . J. Virol. . 70 . 11 . 7734–43 . 1996 . 8892894 . 190843 . 10.1128/JVI.70.11.7734-7743.1996.
• Hecker C, Weise C, Schneider-Schaulies J, Holmes HC, ter Meulen V . Specific binding of HIV-1 envelope protein gp120 to the structural membrane proteins ezrin and moesin . Virus Res. . 49 . 2 . 215–23 . 1997 . 9213396 . 10.1016/S0168-1702(97)00039-7 . 7126478 .
• Serrador JM, Alonso-Lebrero JL, del Pozo MA, Furthmayr H, Schwartz-Albiez R, Calvo J, Lozano F, Sánchez-Madrid F . Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization . J. Cell Biol. . 138 . 6 . 1409–23 . 1997 . 9298994 . 2132557 . 10.1083/jcb.138.6.1409 .
• Reczek D, Berryman M, Bretscher A . Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family . J. Cell Biol. . 139 . 1 . 169–79 . 1997 . 9314537 . 2139813 . 10.1083/jcb.139.1.169 .
• Murthy A, Gonzalez-Agosti C, Cordero E, Pinney D, Candia C, Solomon F, Gusella J, Ramesh V . NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins . J. Biol. Chem. . 273 . 3 . 1273–6 . 1998 . 9430655 . 10.1074/jbc.273.3.1273 . free .
• Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S . Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2 . J. Cell Biol. . 140 . 4 . 885–95 . 1998 . 9472040 . 2141743 . 10.1083/jcb.140.4.885 .

Notes and References

1. Lankes WT, Furthmayr H . Moesin: a member of the protein 4.1-talin-ezrin family of proteins . Proc. Natl. Acad. Sci. U.S.A. . 88 . 19 . 8297–301 . Oct 1991 . 1924289 . 52495 . 10.1073/pnas.88.19.8297 . 1991PNAS...88.8297L . free .
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. . 219 . 1 . 180–96 . Sep 1995 . 7628534 . 10.1006/excr.1995.1218 . free .
3. Web site: Entrez Gene: MSN moesin.
4. Serrador JM, Nieto M, Alonso-Lebrero JL, del Pozo MA, Calvo J, Furthmayr H, Schwartz-Albiez R, Lozano F, González-Amaro R, Sánchez-Mateos P, Sánchez-Madrid F . CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts . Blood . 91 . 12 . 4632–44 . Jun 1998 . 9616160 . 10.1182/blood.V91.12.4632.
5. Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S . Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2 . J. Cell Biol. . 140 . 4 . 885–95 . Feb 1998 . 9472040 . 2141743 . 10.1083/jcb.140.4.885.
6. Serrador JM, Alonso-Lebrero JL, del Pozo MA, Furthmayr H, Schwartz-Albiez R, Calvo J, Lozano F, Sánchez-Madrid F . Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization . J. Cell Biol. . 138 . 6 . 1409–23 . Sep 1997 . 9298994 . 2132557 . 10.1083/jcb.138.6.1409.
7. Serrador JM, Vicente-Manzanares M, Calvo J, Barreiro O, Montoya MC, Schwartz-Albiez R, Furthmayr H, Lozano F, Sánchez-Madrid F . A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting . J. Biol. Chem. . 277 . 12 . 10400–9 . Mar 2002 . 11784723 . 10.1074/jbc.M110694200 . free .
8. Wientjes FB, Reeves EP, Soskic V, Furthmayr H, Segal AW . The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain . Biochem. Biophys. Res. Commun. . 289 . 2 . 382–8 . Nov 2001 . 11716484 . 10.1006/bbrc.2001.5982 .
9. Barreiro O, Yanez-Mo M, Serrador JM, Montoya MC, Vicente-Manzanares M, Tejedor R, Furthmayr H, Sanchez-Madrid F . Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes . J. Cell Biol. . 157 . 7 . 1233–45 . Jun 2002 . 12082081 . 2173557 . 10.1083/jcb.200112126 .
10. Gajate C, Mollinedo F . Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy . J. Biol. Chem. . 280 . 12 . 11641–7 . Mar 2005 . 15659383 . 10.1074/jbc.M411781200 . free .
11. Gary R, Bretscher A . Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site . Mol. Biol. Cell . 6 . 8 . 1061–75 . Aug 1995 . 7579708 . 301263 . 10.1091/mbc.6.8.1061.
12. Gary R, Bretscher A . Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins . Proc. Natl. Acad. Sci. U.S.A. . 90 . 22 . 10846–50 . Nov 1993 . 8248180 . 47875 . 10.1073/pnas.90.22.10846. 1993PNAS...9010846G . free .