モエシン

モエシン(Moesin)は、ヒトではMSN遺伝子によりコードされるタンパク質である^[5][6]。

MSN
PDBに登録されている構造 PDB オルソログ検索: RCSB PDBe PDBj PDBのIDコード一覧 1E5W, 1EF1, 1SGH
識別子
記号	MSN, HEL70, moesin, IMD50
外部ID	OMIM: 309845 MGI: 97167 HomoloGene: 1833 GeneCards: MSN
遺伝子の位置 (ヒト) 染色体 X染色体[1] バンド データ無し 開始点 65,588,377 bp[1] 終点 65,741,931 bp[1]
遺伝子の位置 (マウス) 染色体 X染色体 (マウス)[2] バンド データ無し 開始点 95,139,648 bp[2] 終点 95,212,158 bp[2]
RNA発現パターン さらなる参照発現データ
遺伝子オントロジー 分子機能 • cytoskeletal protein binding • structural constituent of cytoskeleton • 血漿タンパク結合 • actin binding • double-stranded RNA binding • 受容体結合 • プロテインキナーゼ結合 • cell adhesion molecule binding • 酵素結合 細胞の構成要素 • 細胞質 • 小胞 • cell projection • 仮足 • blood microparticle • 膜 • 焦点接着 • 糸状偽足 • ミエリン鞘 • 細胞膜 • apical part of cell • 微絨毛 • uropod • basolateral plasma membrane • apical plasma membrane • perinuclear region of cytoplasm • エキソソーム • 細胞骨格 • microvillus membrane • 細胞核 • 細胞周辺 • 細胞外空間 • cell surface • 細胞質基質 生物学的プロセス • leukocyte 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 process 出典:Amigo / QuickGO
オルソログ
種	ヒト	マウス
Entrez	4478	17698
Ensembl	ENSG00000147065	ENSMUSG00000031207
UniProt	P26038	P26041
RefSeq (mRNA)	NM_002444	NM_010833
RefSeq (タンパク質)	NP_002435	NP_034963
場所 (UCSC)	Chr X: 65.59 – 65.74 Mb	Chr X: 95.14 – 95.21 Mb
PubMed検索	[3]	[4]
ウィキデータ
閲覧/編集 ヒト 閲覧/編集 マウス

Membrane-Organizing Extension Spike proteINの略であり、エズリン、ラディキシンとともにERMファミリーを構成する。ERMファミリーは、アクチンからなる細胞骨格と細胞膜との間の架橋として機能していると考えられている^[7]。

モエシンは、細胞移動のための細胞間認識やシグナル伝達に重要な糸状仮足(フィロポディア)や他の膜質突起に局在する^[7]。

相互作用

モエシンは、以下のタンパク質とタンパク質間相互作用する。

• CD43^[8][9]
• ICAM3^[10][11]
• NCF1^[12]
• NCF4^[12]
• VCAM-1^[13]
• エズリン^[14][15][16]

出典

1. GRCh38: Ensembl release 89: ENSG00000147065 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031207 - Ensembl, May 2017
3. Human PubMed Reference:
4. Mouse PubMed Reference:
5. “Moesin: a member of the protein 4.1-talin-ezrin family of proteins”. Proc. Natl. Acad. Sci. U.S.A. 88 (19): 8297-301. (Oct 1991). doi:10.1073/pnas.88.19.8297. PMC 52495. PMID 1924289. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC52495/.
6. “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. (Sep 1995). doi:10.1006/excr.1995.1218. PMID 7628534.
7. “Entrez Gene: MSN moesin”. 2020年3月31日閲覧。
8. “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. (Jun 1998). PMID 9616160.
9. “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. (Feb 1998). doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141743/.
10. “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. (Sep 1997). doi:10.1083/jcb.138.6.1409. PMC 2132557. PMID 9298994. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132557/.
11. “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. (Mar 2002). doi:10.1074/jbc.M110694200. PMID 11784723.
12. “The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain”. Biochem. Biophys. Res. Commun. 289 (2): 382-8. (Nov 2001). doi:10.1006/bbrc.2001.5982. PMID 11716484.
13. “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. (Jun 2002). doi:10.1083/jcb.200112126. PMC 2173557. PMID 12082081. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173557/.
14. “Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy”. J. Biol. Chem. 280 (12): 11641-7. (Mar 2005). doi:10.1074/jbc.M411781200. PMID 15659383.
15. “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. (Aug 1995). doi:10.1091/mbc.6.8.1061. PMC 301263. PMID 7579708. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC301263/.
16. “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. (Nov 1993). doi:10.1073/pnas.90.22.10846. PMC 47875. PMID 8248180. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC47875/.

関連文献

• “ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction”. Curr. Opin. Cell Biol. 9 (1): 70-5. (1997). doi:10.1016/S0955-0674(97)80154-8. PMID 9013673.
• “The ezrin protein family: membrane-cytoskeleton interactions and disease associations”. Curr. Opin. Cell Biol. 9 (5): 659-66. (1997). doi:10.1016/S0955-0674(97)80119-6. PMID 9330869.
• “Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death”. Cell Death Differ. 12 Suppl 1: 932-41. (2005). doi:10.1038/sj.cdd.4401582. PMID 15818415.
• “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. (1995). doi:10.1091/mbc.6.8.1061. PMC 301263. PMID 7579708. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC301263/.
• “Differential expression of the microspike-associated protein moesin in human tissues”. Eur. J. Cell Biol. 67 (3): 189-98. (1995). PMID 7588875.
• “Physical association of moesin and CD46 as a receptor complex for measles virus”. J. Virol. 69 (4): 2248-56. (1995). PMC 188894. PMID 7884872. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC188894/.
• “Structure and localization on the X chromosome of the gene coding for the human filopodial protein moesin (MSN)”. Genomics 19 (2): 326-33. (1994). doi:10.1006/geno.1994.1065. PMID 8188263.
• “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. (1993). doi:10.1073/pnas.90.22.10846. PMC 47875. PMID 8248180. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC47875/.
• “Moesin: a cell membrane protein linked with susceptibility to measles virus infection” (Submitted manuscript). Virology 198 (1): 265-74. (1994). doi:10.1006/viro.1994.1029. PMID 8259662. https://opus.bibliothek.uni-wuerzburg.de/frontdoor/index/index/docId/5873.
• “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. (1995). doi:10.1074/jbc.270.52.31377. PMID 8537411.
• “Cytoskeletal proteins inside human immunodeficiency virus type 1 virions”. J. Virol. 70 (11): 7734-43. (1996). PMC 190843. PMID 8892894. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC190843/.
• “Specific binding of HIV-1 envelope protein gp120 to the structural membrane proteins ezrin and moesin”. Virus Res. 49 (2): 215-23. (1997). doi:10.1016/S0168-1702(97)00039-7. PMID 9213396.
• “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. (1997). doi:10.1083/jcb.138.6.1409. PMC 2132557. PMID 9298994. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132557/.
• “Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family”. J. Cell Biol. 139 (1): 169-79. (1997). doi:10.1083/jcb.139.1.169. PMC 2139813. PMID 9314537. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139813/.
• “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. (1998). doi:10.1074/jbc.273.3.1273. PMID 9430655.
• “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. (1998). doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141743/.