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Gene Review

MSN  -  moesin

Homo sapiens

Synonyms: Membrane-organizing extension spike protein, Moesin
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Disease relevance of MSN


Psychiatry related information on MSN


High impact information on MSN


Chemical compound and disease context of MSN


Biological context of MSN


Anatomical context of MSN


Associations of MSN with chemical compounds


Physical interactions of MSN

  • Furthermore, our data indicate that moesin is identical to the 77-kDa band that copurifies with ezrin in its isolation from human placenta [Bretscher, A. (1989) J. Cell Biol. 108, 921-930] [23].
  • Our data show that moesin co-immunoprecipitated with PECAM-1 in lysates from thrombin-stimulated, but not resting platelets [27].
  • Biochemical analyses showed that ezrin and moesin coimmunoprecipitated with CD43 in T lymphoblasts [28].
  • Immunoprecipitation showed that moesin coprecipitates with TLR4, a well-known lipopolysaccharide receptor, suggesting an early role of moesin in the formation of the initiation complex for lipopolysaccharide signaling [29].
  • We have previously shown that moesin was not involved in the binding to CD95 [30].

Co-localisations of MSN


Regulatory relationships of MSN

  • Moesin-negative ES cells expressing or not expressing human CD46 formed separate pieces of fragmented syncytia which were torn apart during spreading, whereas ES cells expressing moesin exhibited typical syncytia [31].
  • Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin [14].
  • Pharmacologic disruption of interactions between moesin and F-actin in cells expressing PSGL-1 resulted in a dose-dependent inhibition of rolling on P-selectin [32].
  • These data suggest an important role for moesin in lipopolysaccharide-induced TNF-alpha production, highlighting its importance in lipopolysaccharide-mediated signal transduction [29].
  • Moesin is a widely expressed phospho-protein that links many transmembrane molecules to the cortical actin cytoskeleton [14].
  • We propose that activated moesin promotes F-actin redistribution and CD4-CXCR4 clustering and is also required for efficient X4-tropic HIV-1 infection in permissive lymphocytes [33].

Other interactions of MSN


Analytical, diagnostic and therapeutic context of MSN


  1. Ezrin/radixin/moesin proteins are high affinity targets for ADP-ribosylation by Pseudomonas aeruginosa ExoS. Maresso, A.W., Baldwin, M.R., Barbieri, J.T. J. Biol. Chem. (2004) [Pubmed]
  2. Moesin and CD44 expression in cutaneous melanocytic tumours. Ichikawa, T., Masumoto, J., Kaneko, M., Saida, T., Sagara, J., Taniguchi, S. Br. J. Dermatol. (1998) [Pubmed]
  3. Differential expression of the microspike-associated protein moesin in human tissues. Schwartz-Albiez, R., Merling, A., Spring, H., Möller, P., Koretz, K. Eur. J. Cell Biol. (1995) [Pubmed]
  4. Shifts in cellular localization of moesin in normal oral epithelium, oral epithelial dysplasia, verrucous carcinoma and oral squamous cell carcinoma. Kobayashi, H., Sagara, J., Masumoto, J., Kurita, H., Kurashina, K., Taniguchi, S. J. Oral Pathol. Med. (2003) [Pubmed]
  5. Expression of moesin and its associated molecule CD44 in epithelial skin tumors. Ichikawa, T., Masumoto, J., Kaneko, M., Saida, T., Sagara, J., Taniguchi, S. J. Cutan. Pathol. (1998) [Pubmed]
  6. Specific antibodies to moesin, a membrane-cytoskeleton linker protein, are frequently detected in patients with acquired aplastic anemia. Takamatsu, H., Feng, X., Chuhjo, T., Lu, X., Sugimori, C., Okawa, K., Yamamoto, M., Iseki, S., Nakao, S. Blood (2007) [Pubmed]
  7. Strategy for teaching evaluation research in psychiatric/mental health nursing. Austin, J.K., Opie, N.D., Frazier, H.A. The Journal of nursing education. (1987) [Pubmed]
  8. Consensus for practice in the 21st century: setting a framework. Keane, A. ANNA journal / American Nephrology Nurses' Association. (1995) [Pubmed]
  9. Bringing nursing leadership to shaping state policy: an interview with virginia trotter betts. Keepnews, D.M. Policy, politics & nursing practice. (2006) [Pubmed]
  10. A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor. Trofatter, J.A., MacCollin, M.M., Rutter, J.L., Murrell, J.R., Duyao, M.P., Parry, D.M., Eldridge, R., Kley, N., Menon, A.G., Pulaski, K. Cell (1993) [Pubmed]
  11. A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor. Trofatter, J.A., MacCollin, M.M., Rutter, J.L., Murrell, J.R., Duyao, M.P., Parry, D.M., Eldridge, R., Kley, N., Menon, A.G., Pulaski, K. Cell (1993) [Pubmed]
  12. A role for moesin in polarity. Miller, K.G. Trends Cell Biol. (2003) [Pubmed]
  13. ITAM-based interaction of ERM proteins with Syk mediates signaling by the leukocyte adhesion receptor PSGL-1. Urzainqui, A., Serrador, J.M., Viedma, F., Yáñez-Mó, M., Rodríguez, A., Corbí, A.L., Alonso-Lebrero, J.L., Luque, A., Deckert, M., Vázquez, J., Sánchez-Madrid, F. Immunity (2002) [Pubmed]
  14. Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin. Delon, J., Kaibuchi, K., Germain, R.N. Immunity (2001) [Pubmed]
  15. The merlin tumor suppressor localizes preferentially in membrane ruffles. Gonzalez-Agosti, C., Xu, L., Pinney, D., Beauchamp, R., Hobbs, W., Gusella, J., Ramesh, V. Oncogene (1996) [Pubmed]
  16. Experience of the Belgian Society of Medical Oncology with single-administration 5 g/m2 ifosfamide with mesna as second- or third-line therapy in advanced breast cancer. Paridaens, R., Focan, C., Michel, J., Piccart, M., Salamon, E., Beauduin, M., Closon, M.T., Tueni, E., Vindevoghel, A., Majois, F. Cancer Chemother. Pharmacol. (1990) [Pubmed]
  17. Lysophosphatidic acid-induced platelet shape change proceeds via Rho/Rho kinase-mediated myosin light-chain and moesin phosphorylation. Retzer, M., Essler, M. Cell. Signal. (2000) [Pubmed]
  18. Structure and localization on the X chromosome of the gene coding for the human filopodial protein moesin (MSN). Wilgenbus, K.K., Hsieh, C.L., Lankes, W.T., Milatovich, A., Francke, U., Furthmayr, H. Genomics (1994) [Pubmed]
  19. Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization. Serrador, J.M., Alonso-Lebrero, J.L., del Pozo, M.A., Furthmayr, H., Schwartz-Albiez, R., Calvo, J., Lozano, F., Sánchez-Madrid, F. J. Cell Biol. (1997) [Pubmed]
  20. C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton. Simons, P.C., Pietromonaco, S.F., Reczek, D., Bretscher, A., Elias, L. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  21. The two poles of the lymphocyte: specialized cell compartments for migration and recruitment. del Pozo, M.A., Nieto, M., Serrador, J.M., Sancho, D., Vicente-Manzanares, M., Martínez, C., Sánchez-Madrid, F. Cell Adhes. Commun. (1998) [Pubmed]
  22. Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes. Barreiro, O., Yanez-Mo, M., Serrador, J.M., Montoya, M.C., Vicente-Manzanares, M., Tejedor, R., Furthmayr, H., Sanchez-Madrid, F. J. Cell Biol. (2002) [Pubmed]
  23. Moesin: a member of the protein 4.1-talin-ezrin family of proteins. Lankes, W.T., Furthmayr, H. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  24. The cytoplasmic tail of L-selectin interacts with members of the Ezrin-Radixin-Moesin (ERM) family of proteins: cell activation-dependent binding of Moesin but not Ezrin. Ivetic, A., Deka, J., Ridley, A., Ager, A. J. Biol. Chem. (2002) [Pubmed]
  25. Polarization and interaction of adhesion molecules P-selectin glycoprotein ligand 1 and intercellular adhesion molecule 3 with moesin and ezrin in myeloid cells. Alonso-Lebrero, J.L., Serrador, J.M., Domínguez-Jiménez, C., Barreiro, O., Luque, A., del Pozo, M.A., Snapp, K., Kansas, G., Schwartz-Albiez, R., Furthmayr, H., Lozano, F., Sánchez-Madrid, F. Blood (2000) [Pubmed]
  26. The NF2 tumor suppressor Merlin and the ERM proteins interact with N-WASP and regulate its actin polymerization function. Manchanda, N., Lyubimova, A., Ho, H.Y., James, M.F., Gusella, J.F., Ramesh, N., Snapper, S.B., Ramesh, V. J. Biol. Chem. (2005) [Pubmed]
  27. Platelet moesin interacts with PECAM-1 (CD31). Gamulescu, M.A., Seifert, K., Tingart, M., Falet, H., Hoffmeister, K.M. Platelets (2003) [Pubmed]
  28. CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts. Serrador, J.M., Nieto, M., Alonso-Lebrero, J.L., del Pozo, M.A., Calvo, J., Furthmayr, H., Schwartz-Albiez, R., Lozano, F., González-Amaro, R., Sánchez-Mateos, P., Sánchez-Madrid, F. Blood (1998) [Pubmed]
  29. Role for moesin in lipopolysaccharide-stimulated signal transduction. Iontcheva, I., Amar, S., Zawawi, K.H., Kantarci, A., Van Dyke, T.E. Infect. Immun. (2004) [Pubmed]
  30. Identification and relevance of the CD95-binding domain in the N-terminal region of ezrin. Lozupone, F., Lugini, L., Matarrese, P., Luciani, F., Federici, C., Iessi, E., Margutti, P., Stassi, G., Malorni, W., Fais, S. J. Biol. Chem. (2004) [Pubmed]
  31. Moesin is not a receptor for measles virus entry into mouse embryonic stem cells. Doi, Y., Kurita, M., Matsumoto, M., Kondo, T., Noda, T., Tsukita, S., Tsukita, S., Seya, T. J. Virol. (1998) [Pubmed]
  32. Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin. Snapp, K.R., Heitzig, C.E., Kansas, G.S. Blood (2002) [Pubmed]
  33. Moesin is required for HIV-1-induced CD4-CXCR4 interaction, F-actin redistribution, membrane fusion and viral infection in lymphocytes. Barrero-Villar, M., Cabrero, J.R., Gordón-Alonso, M., Barroso-González, J., Alvarez-Losada, S., Muñoz-Fernández, M.A., Sánchez-Madrid, F., Valenzuela-Fernández, A. J. Cell. Sci. (2009) [Pubmed]
  34. Moesin, the major ERM protein of lymphocytes and platelets, differs from ezrin in its insensitivity to calpain. Shcherbina, A., Bretscher, A., Kenney, D.M., Remold-O'Donnell, E. FEBS Lett. (1999) [Pubmed]
  35. A juxta-membrane amino acid sequence of P-selectin glycoprotein ligand-1 is involved in moesin binding and ezrin/radixin/moesin-directed targeting at the trailing edge of migrating lymphocytes. Serrador, J.M., Urzainqui, A., Alonso-Lebrero, J.L., Cabrero, J.R., Montoya, M.C., Vicente-Manzanares, M., Yáñez-Mó, M., Sánchez-Madrid, F. Eur. J. Immunol. (2002) [Pubmed]
  36. Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins. Gary, R., Bretscher, A. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  37. Insight into the molecular basis of pathogen abundance: group A Streptococcus inhibitor of complement inhibits bacterial adherence and internalization into human cells. Hoe, N.P., Ireland, R.M., DeLeo, F.R., Gowen, B.B., Dorward, D.W., Voyich, J.M., Liu, M., Burns, E.H., Culnan, D.M., Bretscher, A., Musser, J.M. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
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