Moesin

Moesin
PDB rendering based on 1e5w.
Available structures PDB 1E5W, 1EF1, 1SGH
Identifiers
Symbols	MSN;
External IDs	OMIM: 309845 MGI: 97167 HomoloGene: 1833 GeneCards: MSN Gene
Gene Ontology Molecular function • actin binding • receptor binding • structural constituent of cytoskeleton • protein binding • cell adhesion molecule binding Cellular component • uropod • soluble fraction • nucleus • nucleolus • cytoplasm • cytoskeleton • plasma membrane • microvillus • focal adhesion • internal side of plasma membrane • cell surface • basolateral plasma membrane • apical plasma membrane • extrinsic to membrane • filopodium • secretory granule membrane • filopodium membrane • microvillus membrane • apical part of cell Biological process • cellular component movement • leukocyte cell-cell adhesion • membrane to membrane docking • leukocyte migration Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4478	17698
Ensembl	ENSG00000147065	ENSMUSG00000031207
UniProt	P26038	Q05DU4
RefSeq (mRNA)	NM_002444	NM_010833.2
RefSeq (protein)	NP_002435	NP_034963.2
Location (UCSC)	Chr X: 64.89 – 64.96 Mb	Chr X: 93.29 – 93.36 Mb
PubMed search	[1]	[2]

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]

Interactions

Moesin has been shown to interact with CD43,^[4][5] Neutrophil cytosolic factor 1,^[6] VCAM-1,^[7] Neutrophil cytosolic factor 4,^[6] ICAM3^[8][9] and EZR.^[10][11][12]

References

1. ^ Lankes WT, Furthmayr H (Oct 1991). "Moesin: a member of the protein 4.1-talin-ezrin family of proteins". Proc Natl Acad Sci U S A 88 (19): 8297–301. doi:10.1073/pnas.88.19.8297. PMC 52495. PMID 1924289. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=52495. 
2. ^ Amieva MR, Furthmayr H (Sep 1995). "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. doi:10.1006/excr.1995.1218. PMID 7628534. 
3. ^ "Entrez Gene: MSN moesin". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4478. 
4. ^ 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 (Jun. 1998). "CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts". Blood (UNITED STATES) 91 (12): 4632–44. ISSN 0006-4971. PMID 9616160. 
5. ^ Yonemura, S; Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S (Feb. 1998). "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. (UNITED STATES) 140 (4): 885–95. doi:10.1083/jcb.140.4.885. ISSN 0021-9525. PMC 2141743. PMID 9472040. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2141743. 
6. ^ ^{a b} Wientjes, F B; Reeves E P, Soskic V, Furthmayr H, Segal A W (Nov. 2001). "The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain". Biochem. Biophys. Res. Commun. (United States) 289 (2): 382–8. doi:10.1006/bbrc.2001.5982. ISSN 0006-291X. PMID 11716484. 
7. ^ Barreiro, Olga; Yanez-Mo Maria, Serrador Juan M, Montoya Maria C, Vicente-Manzanares Miguel, Tejedor Reyes, Furthmayr Heinz, Sanchez-Madrid Francisco (Jun. 2002). "Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes". J. Cell Biol. (United States) 157 (7): 1233–45. doi:10.1083/jcb.200112126. ISSN 0021-9525. PMC 2173557. PMID 12082081. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173557. 
8. ^ Serrador, J M; Alonso-Lebrero J L, del Pozo M A, Furthmayr H, Schwartz-Albiez R, Calvo J, Lozano F, Sánchez-Madrid F (Sep. 1997). "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. (UNITED STATES) 138 (6): 1409–23. doi:10.1083/jcb.138.6.1409. ISSN 0021-9525. PMC 2132557. PMID 9298994. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2132557. 
9. ^ Serrador, Juan M; Vicente-Manzanares Miguel, Calvo Javier, Barreiro Olga, Montoya Maria C, Schwartz-Albiez Reinhard, Furthmayr Heinz, Lozano Francisco, Sánchez-Madrid Francisco (Mar. 2002). "A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting". J. Biol. Chem. (United States) 277 (12): 10400–9. doi:10.1074/jbc.M110694200. ISSN 0021-9258. PMID 11784723. 
10. ^ Gajate, Consuelo; Mollinedo Faustino (Mar. 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. (United States) 280 (12): 11641–7. doi:10.1074/jbc.M411781200. ISSN 0021-9258. PMID 15659383. 
11. ^ Gary, R; Bretscher A (Aug. 1995). "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 (UNITED STATES) 6 (8): 1061–75. ISSN 1059-1524. PMC 301263. PMID 7579708. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=301263. 
12. ^ Gary, R; Bretscher A (Nov. 1993). "Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 90 (22): 10846–50. doi:10.1073/pnas.90.22.10846. ISSN 0027-8424. PMC 47875. PMID 8248180. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=47875. 

Further reading

• Tsukita S, Yonemura S (1997). "ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction.". Curr. Opin. Cell Biol. 9 (1): 70–5. doi:10.1016/S0955-0674(97)80154-8. PMID 9013673. 
• Vaheri A, Carpén O, Heiska L, et al. (1997). "The ezrin protein family: membrane-cytoskeleton interactions and disease associations.". Curr. Opin. Cell Biol. 9 (5): 659–66. doi:10.1016/S0955-0674(97)80119-6. PMID 9330869. 
• Matarrese P, Malorni W (2006). "Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death.". Cell Death Differ. 12 Suppl 1: 932–41. doi:10.1038/sj.cdd.4401582. PMID 15818415. 
• Gary R, Bretscher A (1995). "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. PMC 301263. PMID 7579708. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=301263. 
• Schwartz-Albiez R, Merling A, Spring H, et al. (1995). "Differential expression of the microspike-associated protein moesin in human tissues.". Eur. J. Cell Biol. 67 (3): 189–98. PMID 7588875. 
• Schneider-Schaulies J, Dunster LM, Schwartz-Albiez R, et al. (1995). "Physical association of moesin and CD46 as a receptor complex for measles virus.". J. Virol. 69 (4): 2248–56. PMC 188894. PMID 7884872. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=188894. 
• Wilgenbus KK, Hsieh CL, Lankes WT, et al. (1994). "Structure and localization on the X chromosome of the gene coding for the human filopodial protein moesin (MSN).". Genomics 19 (2): 326–33. doi:10.1006/geno.1994.1065. PMID 8188263. 
• Gary R, Bretscher A (1993). "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. doi:10.1073/pnas.90.22.10846. PMC 47875. PMID 8248180. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=47875. 
• Dunster LM, Schneider-Schaulies J, Löffler S, et al. (1994). "Moesin: a cell membrane protein linked with susceptibility to measles virus infection.". Virology 198 (1): 265–74. doi:10.1006/viro.1994.1029. PMID 8259662. 
• Nakamura F, Amieva MR, Furthmayr H (1996). "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. doi:10.1074/jbc.270.52.31377. PMID 8537411. 
• Ott DE, Coren LV, Kane BP, et al. (1996). "Cytoskeletal proteins inside human immunodeficiency virus type 1 virions.". J. Virol. 70 (11): 7734–43. PMC 190843. PMID 8892894. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=190843. 
• Hecker C, Weise C, Schneider-Schaulies J, et al. (1997). "Specific binding of HIV-1 envelope protein gp120 to the structural membrane proteins ezrin and moesin.". Virus Res. 49 (2): 215–23. doi:10.1016/S0168-1702(97)00039-7. PMID 9213396. 
• Serrador JM, Alonso-Lebrero JL, del Pozo MA, et al. (1997). "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. doi:10.1083/jcb.138.6.1409. PMC 2132557. PMID 9298994. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2132557. 
• Reczek D, Berryman M, Bretscher A (1998). "Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family.". J. Cell Biol. 139 (1): 169–79. doi:10.1083/jcb.139.1.169. PMC 2139813. PMID 9314537. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2139813. 
• Murthy A, Gonzalez-Agosti C, Cordero E, et al. (1998). "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. doi:10.1074/jbc.273.3.1273. PMID 9430655. 
• Yonemura S, Hirao M, Doi Y, et al. (1998). "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. doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2141743. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.