Moesin

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Moesin
Protein MSN PDB 1e5w.png
PDB rendering based on 1e5w.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbol MSN
External IDs OMIM309845 MGI97167 HomoloGene1833 GeneCards: MSN Gene
RNA expression pattern
PBB GE MSN 200600 at tn.png
More reference expression data
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:
64.89 – 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]

Interactions[edit]

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]

References[edit]

  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.