Moesin

MSN
Available structures PDB Ortholog search: PDBe RCSB 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) [1] Band Xq12 Start 65,588,377 bp [1] End 65,741,931 bp [1]
Gene location (Mouse) Chr. X chromosome (mouse) [2] Band X|X C3 Start 95,139,648 bp [2] End 95,212,158 bp [2]
RNA expression pattern 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 PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Moesin is a protein that in humans is encoded by the MSN gene. ^{[5] [6]}

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. ^[7]

Moesin is localized to filopodia and other membranous protrusions that are important for cell–cell recognition and signaling and for cell movement. ^[7]

Moesin has FERM domain at N-terminal.

Interactions

Moesin has been shown to interact with:

• CD43 ^{[8] [9]}
• ICAM3 ^{[10] [11]}
• Neutrophil cytosolic factor 1, ^[12]
• Neutrophil cytosolic factor 4 ^[12]
• VCAM-1 ^[13]
• EZR ^{[14] [15] [16]}

References

1. GRCh38: Ensembl release 89: ENSG00000147065 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031207 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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. Bibcode:1991PNAS...88.8297L. doi: 10.1073/pnas.88.19.8297 . PMC   52495 . PMID   1924289.
6. 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.
7. "Entrez Gene: MSN moesin".
8. 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 (Jun 1998). "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. doi:10.1182/blood.V91.12.4632. PMID   9616160.
9. 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. 140 (4): 885–95. doi:10.1083/jcb.140.4.885. PMC   2141743 . PMID   9472040.
10. Serrador JM, Alonso-Lebrero JL, del Pozo MA, 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. 138 (6): 1409–23. doi:10.1083/jcb.138.6.1409. PMC   2132557 . PMID   9298994.
11. Serrador JM, Vicente-Manzanares M, Calvo J, Barreiro O, Montoya MC, Schwartz-Albiez R, Furthmayr H, Lozano F, Sánchez-Madrid F (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. 277 (12): 10400–9. doi: 10.1074/jbc.M110694200 . PMID   11784723.
12. Wientjes FB, Reeves EP, Soskic V, Furthmayr H, Segal AW (Nov 2001). "The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain". Biochem. Biophys. Res. Commun. 289 (2): 382–8. doi:10.1006/bbrc.2001.5982. PMID   11716484.
13. Barreiro O, Yanez-Mo M, Serrador JM, Montoya MC, Vicente-Manzanares M, Tejedor R, Furthmayr H, Sanchez-Madrid F (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. 157 (7): 1233–45. doi:10.1083/jcb.200112126. PMC   2173557 . PMID   12082081.
14. Gajate C, Mollinedo F (Mar 2005). "Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy". J. Biol. Chem. 280 (12): 11641–7. doi: 10.1074/jbc.M411781200 . PMID   15659383.
15. 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. 6 (8): 1061–75. doi:10.1091/mbc.6.8.1061. PMC   301263 . PMID   7579708.
16. 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. 90 (22): 10846–50. Bibcode:1993PNAS...9010846G. doi: 10.1073/pnas.90.22.10846 . PMC   47875 . PMID   8248180.

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, 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. PMID   9330869.
• 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 . 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. doi:10.1091/mbc.6.8.1061. PMC   301263 . PMID   7579708.
• 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. PMID   7588875.
• 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. PMC   188894 . PMID   7884872.
• 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 . 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. Bibcode:1993PNAS...9010846G. doi: 10.1073/pnas.90.22.10846 . PMC   47875 . PMID   8248180.
• 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. PMID   8259662.
• 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 . PMID   8537411.
• 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. PMC   190843 . PMID   8892894.
• 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. PMC   7126478 . PMID   9213396.
• 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. PMC   2132557 . PMID   9298994.
• 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. PMC   2139813 . PMID   9314537.
• 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 . PMID   9430655.
• 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. PMC   2141743 . PMID   9472040.

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