Moesin

MSN
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMSN, HEL70, moesin, IMD50
External IDsMGI: 97167 HomoloGene: 1833 GeneCards: MSN
Gene location (Human)
Chr.X chromosome (human)[1]
BandNo data availableStart65,588,377 bp[1]
End65,741,931 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr X: 96.1 – 96.17 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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]

Interactions

Moesin has been shown to interact with:

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000147065 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031207 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  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. PMC 52495 Freely accessible. PMID 1924289. doi:10.1073/pnas.88.19.8297.
  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. PMID 7628534. doi:10.1006/excr.1995.1218.
  7. 1 2 "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. 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. PMC 2141743 Freely accessible. PMID 9472040. doi:10.1083/jcb.140.4.885.
  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. PMC 2132557 Freely accessible. PMID 9298994. doi:10.1083/jcb.138.6.1409.
  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. PMID 11784723. doi:10.1074/jbc.M110694200.
  12. 1 2 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. PMID 11716484. doi:10.1006/bbrc.2001.5982.
  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. PMC 2173557 Freely accessible. PMID 12082081. doi:10.1083/jcb.200112126.
  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. PMID 15659383. doi:10.1074/jbc.M411781200.
  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. PMC 301263 Freely accessible. PMID 7579708. doi:10.1091/mbc.6.8.1061.
  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. PMC 47875 Freely accessible. PMID 8248180. doi:10.1073/pnas.90.22.10846.

Further reading

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