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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:


  1. ^ Lankes W, 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 M, 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, Nieto M, Alonso-Lebrero J, del Pozo M, Calvo J, Furthmayr H et al. (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. PMID 9616160. 
  5. ^ Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S et al. (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. PMC 2141743. PMID 9472040. 
  6. ^ Serrador J, Alonso-Lebrero J, del Pozo M, Furthmayr H, Schwartz-Albiez R, Calvo J et al. (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. PMC 2132557. PMID 9298994. 
  7. ^ Serrador J, Vicente-Manzanares M, Calvo J, Barreiro O, Montoya M, Schwartz-Albiez R et al. (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. 
  8. ^ a b Wientjes F, Reeves E, Soskic V, Furthmayr H, Segal A (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. 
  9. ^ Barreiro O, Yanez-Mo M, Serrador J, Montoya M, Vicente-Manzanares M, Tejedor R et al. (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. 
  10. ^ 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. 
  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 6 (8): 1061–75. 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. 90 (22): 10846–50. 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.