Moesin

Moesin
File:PBB Protein MSN image.jpg PDB rendering based on 1e5w.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1e5w​, 1ef1​, 1j19​, 1sgh​, 2d10​, 2d11​, 2d2q​, 2yvc​
Identifiers
Symbols	MSN ;
External IDs	Template:OMIM5 Template:MGI HomoloGene: 1833
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
File:PBB GE MSN 200600 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Moesin, also known as MSN, is a human gene.

Moesin (for membrane-organizing extension spike protein) is a member of the ERM 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.

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. 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. PMID 9330869.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.
• Lankes WT, Furthmayr H (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. PMID 1924289.
• 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. PMID 7579708.
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Amieva MR, Furthmayr H (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.
• 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. PMID 7884872.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 8248180.
• 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. PMID 8259662.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 8537411.CS1 maint: Multiple names: authors list (link)
• Ott DE, Coren LV, Kane BP; et al. (1996). "Cytoskeletal proteins inside human immunodeficiency virus type 1 virions". J. Virol. 70 (11): 7734–43. PMID 8892894.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 9213396.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 9298994.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 9314537.CS1 maint: Multiple names: authors list (link)
• 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. PMID 9430655.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 9472040.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)

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