Moesin

Last updated
MSN
Protein MSN PDB 1e5w.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases MSN , HEL70, moesin, IMD50
External IDs OMIM: 309845 MGI: 97167 HomoloGene: 1833 GeneCards: MSN
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002444

NM_010833

RefSeq (protein)

NP_002435

NP_034963

Location (UCSC) Chr X: 65.59 – 65.74 Mb Chr X: 95.14 – 95.21 Mb
PubMed search [3] [4]
Wikidata
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Moesin is a protein that in humans is encoded by the MSN gene. [5] [6]

Contents

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

Moesin has been shown to interact with:

Related Research Articles

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<span class="mw-page-title-main">Tight junction protein 1</span> Protein found in humans

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<span class="mw-page-title-main">ICAM3</span> Mammalian protein found in Homo sapiens

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<span class="mw-page-title-main">CLDN1</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">ICAM2</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Radixin</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">ARHGDIA</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">MYLIP</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Catenin alpha-1</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">ERM protein family</span> Protein family

The ERM protein family consists of three closely related proteins, ezrin, radixin and moesin. The three paralogs, ezrin, radixin and moesin, are present in vertebrates, whereas other species have only one ERM gene. Therefore, in vertebrates these paralogs likely arose by gene duplication.

<span class="mw-page-title-main">FERM domain</span>

In molecular biology, the FERM domain is a widespread protein module involved in localising proteins to the plasma membrane. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus in the majority of proteins in which it is found.

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:". 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. 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. 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. 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. 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

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