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Wikipedia

Moesin

January 01, 1970

Moesin is a protein that in humans is encoded by the MSN gene.[5][6]

MSN
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMSN, HEL70, moesin, IMD50
External IDsOMIM: 309845 MGI: 97167 HomoloGene: 1833 GeneCards: MSN
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: 95.14 – 95.21 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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]

Moesin has FERM domain at N-terminal.

Interactions edit

Moesin has been shown to interact with:

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000147065 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031207 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  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. Bibcode:1991PNAS...88.8297L. doi:10.1073/pnas.88.19.8297. PMC 52495. PMID 1924289.
  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. doi:10.1006/excr.1995.1218. PMID 7628534.
  7. ^ a b "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. doi:10.1182/blood.V91.12.4632. 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. doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040.
  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. doi:10.1083/jcb.138.6.1409. PMC 2132557. PMID 9298994.
  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. doi:10.1074/jbc.M110694200. PMID 11784723.
  12. ^ a b 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. doi:10.1006/bbrc.2001.5982. PMID 11716484.
  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. doi:10.1083/jcb.200112126. PMC 2173557. PMID 12082081.
  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. doi:10.1074/jbc.M411781200. PMID 15659383.
  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. doi:10.1091/mbc.6.8.1061. PMC 301263. PMID 7579708.
  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. Bibcode:1993PNAS...9010846G. doi:10.1073/pnas.90.22.10846. PMC 47875. PMID 8248180.

Further reading edit

  • Tsukita S, Yonemura S (1997). "ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction". Curr. Opin. Cell Biol. 9 (1): 70–5. doi:10.1016/S0955-0674(97)80154-8. PMID 9013673.
  • Vaheri A, Carpén O, Heiska L, Helander TS, Jääskeläinen J, Majander-Nordenswan P, Sainio M, Timonen T, Turunen O (1997). "The ezrin protein family: membrane-cytoskeleton interactions and disease associations". Curr. Opin. Cell Biol. 9 (5): 659–66. doi:10.1016/S0955-0674(97)80119-6. PMID 9330869.
  • Matarrese P, Malorni W (2005). "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.
  • 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. doi:10.1091/mbc.6.8.1061. PMC 301263. PMID 7579708.
  • Schwartz-Albiez R, Merling A, Spring H, Möller P, Koretz K (1995). "Differential expression of the microspike-associated protein moesin in human tissues". Eur. J. Cell Biol. 67 (3): 189–98. PMID 7588875.
  • Schneider-Schaulies J, Dunster LM, Schwartz-Albiez R, Krohne G, ter Meulen V (1995). "Physical association of moesin and CD46 as a receptor complex for measles virus". J. Virol. 69 (4): 2248–56. doi:10.1128/JVI.69.4.2248-2256.1995. PMC 188894. PMID 7884872.
  • Wilgenbus KK, Hsieh CL, Lankes WT, Milatovich A, Francke U, Furthmayr H (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.
  • 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. Bibcode:1993PNAS...9010846G. doi:10.1073/pnas.90.22.10846. PMC 47875. PMID 8248180.
  • Dunster LM, Schneider-Schaulies J, Löffler S, Lankes W, Schwartz-Albiez R, Lottspeich F, ter Meulen V (1994). "Moesin: a cell membrane protein linked with susceptibility to measles virus infection". Virology. 198 (1): 265–74. doi:10.1006/viro.1994.1029. PMID 8259662.
  • Nakamura F, Amieva MR, Furthmayr H (1995). "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. doi:10.1074/jbc.270.52.31377. PMID 8537411.
  • Ott DE, Coren LV, Kane BP, Busch LK, Johnson DG, Sowder RC, Chertova EN, Arthur LO, Henderson LE (1996). "Cytoskeletal proteins inside human immunodeficiency virus type 1 virions". J. Virol. 70 (11): 7734–43. doi:10.1128/JVI.70.11.7734-7743.1996. PMC 190843. PMID 8892894.
  • Hecker C, Weise C, Schneider-Schaulies J, Holmes HC, ter Meulen V (1997). "Specific binding of HIV-1 envelope protein gp120 to the structural membrane proteins ezrin and moesin". Virus Res. 49 (2): 215–23. doi:10.1016/S0168-1702(97)00039-7. PMC 7126478. PMID 9213396.
  • Serrador JM, Alonso-Lebrero JL, del Pozo MA, Furthmayr H, Schwartz-Albiez R, Calvo J, Lozano F, Sánchez-Madrid F (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. doi:10.1083/jcb.138.6.1409. PMC 2132557. PMID 9298994.
  • Reczek D, Berryman M, Bretscher A (1997). "Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family". J. Cell Biol. 139 (1): 169–79. doi:10.1083/jcb.139.1.169. PMC 2139813. PMID 9314537.
  • Murthy A, Gonzalez-Agosti C, Cordero E, Pinney D, Candia C, Solomon F, Gusella J, Ramesh V (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. doi:10.1074/jbc.273.3.1273. PMID 9430655.
  • Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S (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. doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040.

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

January 01, 1970
moesin, protein, that, humans, encoded, gene, msnavailable, structurespdbortholog, search, pdbe, rcsblist, codes1e5w, 1ef1, 1sghidentifiersaliasesmsn, hel70, moesin, imd50external, idsomim, 309845, 97167, homologene, 1833, genecards, msngene, location, human, . Moesin is a protein that in humans is encoded by the MSN gene 5 6 MSNAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes1E5W 1EF1 1SGHIdentifiersAliasesMSN HEL70 moesin IMD50External IDsOMIM 309845 MGI 97167 HomoloGene 1833 GeneCards MSNGene location Human Chr X chromosome human 1 BandXq12Start65 588 377 bp 1 End65 741 931 bp 1 Gene location Mouse Chr X chromosome mouse 2 BandX X C3Start95 139 648 bp 2 End95 212 158 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inlower lobe of lungmonocytesynovial jointsaphenous veinsynovial membraneright lungappendixsmooth muscle tissueupper lobe of lungbloodTop expressed inright lungright lung lobeleft lungleft lung lobeascending aortaaortic valvespleenanklebloodcalvariaMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functioncytoskeletal protein binding structural constituent of cytoskeleton protein binding actin binding double stranded RNA binding signaling receptor binding protein kinase binding cell adhesion molecule binding enzyme bindingCellular componentcytoplasm vesicle cell projection pseudopodium blood microparticle membrane focal adhesion filopodium myelin sheath plasma membrane apical part of cell microvillus uropod basolateral plasma membrane apical plasma membrane perinuclear region of cytoplasm extracellular exosome cytoskeleton microvillus membrane nucleus cell periphery extracellular space cell surface cytosolBiological processleukocyte cell cell adhesion regulation of cell size establishment of endothelial barrier regulation of organelle assembly cellular response to testosterone stimulus regulation of lymphocyte migration positive regulation of podosome assembly gland morphogenesis positive regulation of gene expression establishment of epithelial cell apical basal polarity regulation of cell shape membrane to membrane docking positive regulation of protein localization to early endosome positive regulation of early endosome to late endosome transport leukocyte migration cytoskeleton organization immunological synapse formation T cell proliferation T cell aggregation T cell migration interleukin 12 mediated signaling pathway viral processSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez447817698EnsemblENSG00000147065ENSMUSG00000031207UniProtP26038P26041RefSeq mRNA NM 002444NM 010833RefSeq protein NP 002435NP 034963Location UCSC Chr X 65 59 65 74 MbChr X 95 14 95 21 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse 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 Moesin has FERM domain at N terminal Interactions editMoesin has been shown to interact with CD43 8 9 ICAM3 10 11 Neutrophil cytosolic factor 1 12 Neutrophil cytosolic factor 4 12 VCAM 1 13 EZR 14 15 16 References edit a b c GRCh38 Ensembl release 89 ENSG00000147065 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000031207 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine 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 Bibcode 1991PNAS 88 8297L doi 10 1073 pnas 88 19 8297 PMC 52495 PMID 1924289 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 a b Entrez Gene MSN moesin Serrador JM Nieto M Alonso Lebrero JL del Pozo MA Calvo J Furthmayr H Schwartz Albiez R Lozano F Gonzalez Amaro R Sanchez Mateos P Sanchez 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 doi 10 1182 blood V91 12 4632 PMID 9616160 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 doi 10 1083 jcb 140 4 885 PMC 2141743 PMID 9472040 Serrador JM Alonso Lebrero JL del Pozo MA Furthmayr H Schwartz Albiez R Calvo J Lozano F Sanchez 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 doi 10 1083 jcb 138 6 1409 PMC 2132557 PMID 9298994 Serrador JM Vicente Manzanares M Calvo J Barreiro O Montoya MC Schwartz Albiez R Furthmayr H Lozano F Sanchez 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 doi 10 1074 jbc M110694200 PMID 11784723 a b 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 doi 10 1006 bbrc 2001 5982 PMID 11716484 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 doi 10 1083 jcb 200112126 PMC 2173557 PMID 12082081 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 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 doi 10 1091 mbc 6 8 1061 PMC 301263 PMID 7579708 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 Bibcode 1993PNAS 9010846G doi 10 1073 pnas 90 22 10846 PMC 47875 PMID 8248180 Further reading editTsukita S Yonemura S 1997 ERM ezrin radixin moesin family from cytoskeleton to signal transduction Curr Opin Cell Biol 9 1 70 5 doi 10 1016 S0955 0674 97 80154 8 PMID 9013673 Vaheri A Carpen O Heiska L Helander TS Jaaskelainen J Majander Nordenswan P Sainio M Timonen T Turunen O 1997 The ezrin protein family membrane cytoskeleton interactions and disease associations Curr Opin Cell Biol 9 5 659 66 doi 10 1016 S0955 0674 97 80119 6 PMID 9330869 Matarrese P Malorni W 2005 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 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 doi 10 1091 mbc 6 8 1061 PMC 301263 PMID 7579708 Schwartz Albiez R Merling A Spring H Moller P Koretz K 1995 Differential expression of the microspike associated protein moesin in human tissues Eur J Cell Biol 67 3 189 98 PMID 7588875 Schneider Schaulies J Dunster LM Schwartz Albiez R Krohne G ter Meulen V 1995 Physical association of moesin and CD46 as a receptor complex for measles virus J Virol 69 4 2248 56 doi 10 1128 JVI 69 4 2248 2256 1995 PMC 188894 PMID 7884872 Wilgenbus KK Hsieh CL Lankes WT Milatovich A Francke U Furthmayr H 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 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 Bibcode 1993PNAS 9010846G doi 10 1073 pnas 90 22 10846 PMC 47875 PMID 8248180 Dunster LM Schneider Schaulies J Loffler S Lankes W Schwartz Albiez R Lottspeich F ter Meulen V 1994 Moesin a cell membrane protein linked with susceptibility to measles virus infection Virology 198 1 265 74 doi 10 1006 viro 1994 1029 PMID 8259662 Nakamura F Amieva MR Furthmayr H 1995 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 doi 10 1074 jbc 270 52 31377 PMID 8537411 Ott DE Coren LV Kane BP Busch LK Johnson DG Sowder RC Chertova EN Arthur LO Henderson LE 1996 Cytoskeletal proteins inside human immunodeficiency virus type 1 virions J Virol 70 11 7734 43 doi 10 1128 JVI 70 11 7734 7743 1996 PMC 190843 PMID 8892894 Hecker C Weise C Schneider Schaulies J Holmes HC ter Meulen V 1997 Specific binding of HIV 1 envelope protein gp120 to the structural membrane proteins ezrin and moesin Virus Res 49 2 215 23 doi 10 1016 S0168 1702 97 00039 7 PMC 7126478 PMID 9213396 Serrador JM Alonso Lebrero JL del Pozo MA Furthmayr H Schwartz Albiez R Calvo J Lozano F Sanchez Madrid F 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 doi 10 1083 jcb 138 6 1409 PMC 2132557 PMID 9298994 Reczek D Berryman M Bretscher A 1997 Identification of EBP50 A PDZ containing phosphoprotein that associates with members of the ezrin radixin moesin family J Cell Biol 139 1 169 79 doi 10 1083 jcb 139 1 169 PMC 2139813 PMID 9314537 Murthy A Gonzalez Agosti C Cordero E Pinney D Candia C Solomon F Gusella J Ramesh V 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 doi 10 1074 jbc 273 3 1273 PMID 9430655 Yonemura S Hirao M Doi Y Takahashi N Kondo T Tsukita S Tsukita S 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 doi 10 1083 jcb 140 4 885 PMC 2141743 PMID 9472040 This article incorporates text from the United States National Library of Medicine which is in the public domain Retrieved from https en wikipedia org w index php title Moesin amp oldid 1202901829, wikipedia, wiki, book, books, library,

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