From Wikipedia, the free encyclopedia
Jump to: navigation, search
Protein MSN PDB 1e5w.png
PDB rendering based on 1e5w.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols MSN ; HEL70
External IDs OMIM309845 MGI97167 HomoloGene1833 GeneCards: MSN Gene
RNA expression pattern
PBB GE MSN 200600 at tn.png
More reference expression data
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:
64.81 – 64.96 Mb
Chr X:
96.1 – 96.17 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]


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]


  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. 
  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". 
  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. 
  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. 
  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. 
  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. doi:10.1091/mbc.6.8.1061. ISSN 1059-1524. PMC 301263. PMID 7579708. 
  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. 

Further reading[edit]

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