Moesin

MSN
Available structures PDB Ortholog search:PDBeRCSB List of PDB id codes 1E5W,1EF1,1SGH
Identifiers
Aliases	MSN,HEL70, moesin, IMD50
External IDs	OMIM:309845;MGI:97167;HomoloGene:1833;GeneCards:MSN;OMA:MSN - orthologs
Gene location (Human) Chr. X chromosome (human) Band Xq12 Start 65,588,377bp End 65,741,931bp
Gene location (Mouse) Chr. X chromosome (mouse) Band X|X C3 Start 95,139,648bp End 95,212,158bp
RNA expressionpattern Bgee Human Mouse(ortholog) Top expressed in lower lobe of lung white blood cell monocyte granulocyte synovial joint saphenous vein synovial membrane right lung appendix smooth muscle tissue Top expressed in right lung right lung lobe left lung endothelial cell of lymphatic vessel left lung lobe granulocyte mesenteric lymph nodes stroma of bone marrow ascending aorta tibiofemoral joint More reference expression data BioGPS More reference expression data
Gene ontology Molecular function cytoskeletal protein binding structural constituent of cytoskeleton protein binding actin binding double-stranded RNA binding signaling receptor binding protein kinase binding cell adhesion molecule binding enzyme binding Cellular component cytoplasm vesicle cell projection pseudopodium blood microparticle membrane focal adhesion filopodium myelin sheath plasma membrane apical part of cell microvillus uropod basolateral plasma membrane apical plasma membrane perinuclear region of cytoplasm extracellular exosome cytoskeleton microvillus membrane nucleus cell periphery extracellular space cell surface cytosol Biological process leukocyte cell-cell adhesion regulation of cell size establishment of endothelial barrier regulation of organelle assembly cellular response to testosterone stimulus regulation of lymphocyte migration positive regulation of podosome assembly gland morphogenesis positive regulation of gene expression establishment of epithelial cell apical/basal polarity regulation of cell shape membrane to membrane docking positive regulation of protein localization to early endosome positive regulation of early endosome to late endosome transport leukocyte migration cytoskeleton organization immunological synapse formation T cell proliferation T cell aggregation T cell migration interleukin-12-mediated signaling pathway viral process Sources:Amigo/QuickGO
Orthologs Species Human Mouse Entrez 4478 17698 Ensembl ENSG00000147065 ENSMUSG00000031207 UniProt P26038 P26041 RefSeq (mRNA) NM_002444 NM_010833 RefSeq (protein) NP_002435 NP_034963 Location (UCSC) Chr X: 65.59 – 65.74 Mb Chr X: 95.14 – 95.21 Mb PubMedsearch
Wikidata
View/Edit Human View/Edit Mouse

Moesinis aproteinthat in humans is encoded by theMSNgene.

Moesin (for membrane-organizing extension spike protein) is a member of theERM protein familywhich includesezrinandradixin.ERM proteins appear to function as cross-linkers betweenplasma membranesandactin-basedcytoskeletons.

Moesin is localized tofilopodiaand other membranous protrusions that are important forcell–cell recognitionand signaling and for cell movement.

Moesin hasFERM domainatN-terminal.

Interactions

Moesin has been shown tointeractwith:

• CD43
• ICAM3
• Neutrophil cytosolic factor 1,
• Neutrophil cytosolic factor 4
• VCAM-1
• EZR

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.PMID9013673.
• Vaheri A, Carpén O, Heiska L, Helander TS, Jääskeläinen J, Majander-Nordenswan P, Sainio M, Timonen T, Turunen O (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.PMID9330869.
• Matarrese P, Malorni W (2005)."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.PMID15818415.
• 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.doi:10.1091/mbc.6.8.1061.PMC301263.PMID7579708.
• Schwartz-Albiez R, Merling A, Spring H, Möller P, Koretz K (1995). "Differential expression of the microspike-associated protein moesin in human tissues".Eur. J. Cell Biol.67(3): 189–98.PMID7588875.
• Schneider-Schaulies J, Dunster LM, Schwartz-Albiez R, Krohne G, ter Meulen V (1995)."Physical association of moesin and CD46 as a receptor complex for measles virus".J. Virol.69(4): 2248–56.doi:10.1128/JVI.69.4.2248-2256.1995.PMC188894.PMID7884872.
• Wilgenbus KK, Hsieh CL, Lankes WT, Milatovich A, Francke U, Furthmayr H (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.PMID8188263.
• 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.Bibcode:1993PNAS...9010846G.doi:10.1073/pnas.90.22.10846.PMC47875.PMID8248180.
• Dunster LM, Schneider-Schaulies J, Löffler S, Lankes W, Schwartz-Albiez R, Lottspeich F, ter Meulen V (1994)."Moesin: a cell membrane protein linked with susceptibility to measles virus infection".Virology.198(1): 265–74.doi:10.1006/viro.1994.1029.PMID8259662.
• Nakamura F, Amieva MR, Furthmayr H (1995)."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.PMID8537411.
• Ott DE, Coren LV, Kane BP, Busch LK, Johnson DG, Sowder RC, Chertova EN, Arthur LO, Henderson LE (1996)."Cytoskeletal proteins inside human immunodeficiency virus type 1 virions".J. Virol.70(11): 7734–43.doi:10.1128/JVI.70.11.7734-7743.1996.PMC190843.PMID8892894.
• Hecker C, Weise C, Schneider-Schaulies J, Holmes HC, ter Meulen V (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.PMC7126478.PMID9213396.
• Serrador JM, Alonso-Lebrero JL, del Pozo MA, Furthmayr H, Schwartz-Albiez R, Calvo J, Lozano F, Sánchez-Madrid F (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.PMC2132557.PMID9298994.
• Reczek D, Berryman M, Bretscher A (1997)."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.PMC2139813.PMID9314537.
• Murthy A, Gonzalez-Agosti C, Cordero E, Pinney D, Candia C, Solomon F, Gusella J, Ramesh V (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.PMID9430655.
• Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S (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.PMC2141743.PMID9472040.

This article incorporates text from theUnited States National Library of Medicine,which is in thepublic domain.