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Volumn 32, Issue 6, 2003, Pages 344-349

Shifts in cellular localization of moesin in normal oral epithelium, oral epithelial dysplasia, verrucous carcinoma and oral squamous cell carcinoma

Author keywords

Dysplastic lesion; ERM; Immunohistochemistry; Moesin; Oral mucosa; Oral squamous cell carcinoma

Indexed keywords

MOESIN;

EID: 0038466073     PISSN: 09042512     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-0714.2003.00111.x     Document Type: Article
Times cited : (23)

References (30)
  • 1
    • 0031081475 scopus 로고    scopus 로고
    • ERM proteins: Head-to-tail regulation of actin-plasma membrane interaction
    • Tsukita Sa, Yonemura S, Tsukita Sh. ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem Sci 1997; 22: 53-8.
    • (1997) Trends Biochem Sci , vol.22 , pp. 53-58
    • Tsukita, Sa.1    Yonemura, S.2    Tsukita, Sh.3
  • 2
    • 0031043523 scopus 로고    scopus 로고
    • ERM (ezrin/radixin/moesin) family: From cytoskeleton to signal transduction
    • Tsukita Sa, Yonemura S, Tsukita Sh. ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction. Curr Opin Cell Biol 1997; 9: 70-5.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 70-75
    • Tsukita, Sa.1    Yonemura, S.2    Tsukita, Sh.3
  • 3
    • 0023952245 scopus 로고
    • A heparin-binding protein involved in inhibition of smooth muscle cell proliferation
    • Lankes W, Griesmacher A, Grunwald J, Achwartz-Albiez R, Keller R. A heparin-binding protein involved in inhibition of smooth muscle cell proliferation. Biochem J 1988; 251: 831-42.
    • (1988) Biochem J , vol.251 , pp. 831-842
    • Lankes, W.1    Griesmacher, A.2    Grunwald, J.3    Achwartz-Albiez, R.4    Keller, R.5
  • 4
    • 0026091353 scopus 로고
    • Moesin: A member of protein 4.1-talinezrin family of protein
    • Lankes WT, Furthmayr H. Moesin: a member of protein 4.1-talinezrin family of protein. Proc Natl Acad Sci USA 1991; 88: 8297-301.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8297-8301
    • Lankes, W.T.1    Furthmayr, H.2
  • 5
    • 0026802046 scopus 로고
    • A gene family consisting of ezrin, radixin, and moesin. Its specific localization at actin filament/plasma membrane association sites
    • Sato N, Funayama N, Nagafuchi A, Yonemura S, Tsukita Sa, Tsukita Sh. A gene family consisting of ezrin, radixin, and moesin. Its specific localization at actin filament/plasma membrane association sites. J Cell Sci 1992; 103: 131-43.
    • (1992) J Cell Sci , vol.103 , pp. 131-143
    • Sato, N.1    Funayama, N.2    Nagafuchi, A.3    Yonemura, S.4    Tsukita, Sa.5    Tsukita, Sh.6
  • 6
    • 0024814175 scopus 로고
    • cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to 4.1
    • Gould KL, Bretscher A, Esch FS, Hunter T. cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to 4.1. EMBO J 1989; 8: 4133-42.
    • (1989) EMBO J , vol.8 , pp. 4133-4142
    • Gould, K.L.1    Bretscher, A.2    Esch, F.S.3    Hunter, T.4
  • 8
    • 0032559637 scopus 로고    scopus 로고
    • 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
    • Yonemura S, Hirao M, Doi Y, et al. 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 1998; 140: 885-95.
    • (1998) J Cell Biol , vol.140 , pp. 885-895
    • Yonemura, S.1    Hirao, M.2    Doi, Y.3
  • 9
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
    • Tsukita Sa, Oishi K, Sato N, Sagara J, Kawai A, Tsukita Sh. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J Cell Biol 1994; 126: 391-401.
    • (1994) J Cell Biol , vol.126 , pp. 391-401
    • Tsukita, Sa.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5    Tsukita, Sh.6
  • 10
    • 0030847406 scopus 로고    scopus 로고
    • Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistribution to the uropod of T lymphocytes during cell polarization
    • Serrador JM, Alonso-Lebrero JL, del Pozo MA, et al. Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistribution to the uropod of T lymphocytes during cell polarization. J Cell Biol 1997; 138: 1409-23.
    • (1997) J Cell Biol , vol.138 , pp. 1409-1423
    • Serrador, J.M.1    Alonso-Lebrero, J.L.2    Del Pozo, M.A.3
  • 11
    • 0032555599 scopus 로고    scopus 로고
    • Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2)
    • Heiska L, Alfhan K, Gronholm M, Vija P, Vaheri A, Carpen O. Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). J Biol Chem 1998; 273: 21893-900.
    • (1998) J Biol Chem , vol.273 , pp. 21893-21900
    • Heiska, L.1    Alfhan, K.2    Gronholm, M.3    Vija, P.4    Vaheri, A.5    Carpen, O.6
  • 12
    • 0027933858 scopus 로고
    • Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family
    • Turnen O, Wahlstrom T, Vaheri A. Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family. J Cell Biol 1994; 126: 1445-53.
    • (1994) J Cell Biol , vol.126 , pp. 1445-1453
    • Turnen, O.1    Wahlstrom, T.2    Vaheri, A.3
  • 13
    • 0029086637 scopus 로고
    • Subcellular localzation of moesin in dynamic filoponda, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts
    • Amieva MR, Furthmayr H. Subcellular localzation of moesin in dynamic filoponda, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts. Exp Cell Res 1995; 219: 180-96.
    • (1995) Exp Cell Res , vol.219 , pp. 180-196
    • Amieva, M.R.1    Furthmayr, H.2
  • 14
    • 0029116771 scopus 로고
    • Differential expression of the microspike-associated protein moesin in human tissues
    • Schwartz-Albeiz R, Merling A, Spring H, Moller P, Koretz K. Differential expression of the microspike-associated protein moesin in human tissues. Eur J Cell Biol 1995; 67: 189-98.
    • (1995) Eur J Cell Biol , vol.67 , pp. 189-198
    • Schwartz-Albeiz, R.1    Merling, A.2    Spring, H.3    Moller, P.4    Koretz, K.5
  • 18
    • 0025736018 scopus 로고
    • Radixin, abarbed end-capping actin-modulating protein, is concentrated at the cleavage furrow during cytokinesis
    • Sato N, Yonemura S, Obinata T, Tsukita Sa, Tsukita Sh. Radixin, abarbed end-capping actin-modulating protein, is concentrated at the cleavage furrow during cytokinesis. J Cell Biol 1991; 113: 321-30.
    • (1991) J Cell Biol , vol.113 , pp. 321-330
    • Sato, N.1    Yonemura, S.2    Obinata, T.3    Tsukita, Sa.4    Tsukita, Sh.5
  • 21
    • 0027196725 scopus 로고
    • The ezrin-like family of tyrosine kinase substrates: Receptor-specific pattern of tyrosine phosphorylation and relationship to malignant transformation
    • Fazioli F, Wong WT, Ullrich SJ, Sakaguchi K, Appella E, Di Fiore PP. The ezrin-like family of tyrosine kinase substrates: receptor-specific pattern of tyrosine phosphorylation and relationship to malignant transformation. Oncogene 1993; 8: 1335-45.
    • (1993) Oncogene , vol.8 , pp. 1335-1345
    • Fazioli, F.1    Wong, W.T.2    Ullrich, S.J.3    Sakaguchi, K.4    Appella, E.5    Di Fiore, P.P.6
  • 22
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain that includes the F-actin binding site
    • Gray R, Bretscher A. Ezrin self-association involves binding of an N-terminal domain that includes the F-actin binding site. Mol Biol Cell 1995; 6: 1061-75.
    • (1995) Mol Biol Cell , vol.6 , pp. 1061-1075
    • Gray, R.1    Bretscher, A.2
  • 23
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanisms of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao M, Sato N, Kondo T, et al. Regulation mechanisms of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J Cell Biol 1996; 135: 37-51.
    • (1996) J Cell Biol , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3
  • 24
    • 0032498528 scopus 로고    scopus 로고
    • Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/ moesin (ERM) proteins and regulates their head-to-tail association
    • Matsui T, Maeda M, Doi Y, et al. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/ moesin (ERM) proteins and regulates their head-to-tail association. J Cell Biol 1998; 140: 647-57.
    • (1998) J Cell Biol , vol.140 , pp. 647-657
    • Matsui, T.1    Maeda, M.2    Doi, Y.3
  • 25
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration
    • Kajita M, Itoh Y, Chiba T, et al. Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J Cell Biol 2001; 153: 893-904.
    • (2001) J Cell Biol , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3
  • 26
    • 0032830907 scopus 로고    scopus 로고
    • Ezrin regulates cell-cell and cell-matrix adhesion, a possible role with E-cadherin/β-catenin
    • Hiscox S, Jiang WG. Ezrin regulates cell-cell and cell-matrix adhesion, a possible role with E-cadherin/β-catenin. J Cell Sci 1999; 112: 3081-90.
    • (1999) J Cell Sci , vol.112 , pp. 3081-3090
    • Hiscox, S.1    Jiang, W.G.2
  • 28
    • 0032708603 scopus 로고    scopus 로고
    • Ezrin, a membrane-cytoskeletal linking protein, is involved in the process of invasion of endometrial cancer cell
    • Ohtani K, Sakamoto H, Rutherford T, Chen Z, Satoh K, Naftolin F. Ezrin, a membrane-cytoskeletal linking protein, is involved in the process of invasion of endometrial cancer cell. Cancer Lett 1999; 147: 31-8.
    • (1999) Cancer Lett , vol.147 , pp. 31-38
    • Ohtani, K.1    Sakamoto, H.2    Rutherford, T.3    Chen, Z.4    Satoh, K.5    Naftolin, F.6
  • 29
  • 30
    • 0030022505 scopus 로고    scopus 로고
    • Ezrin expression in stromal cells of capillary hemangioblastoma. An immunohistochemical survey of brain tumors
    • Bohling T, Turunen O, Jaaskelainen J, et al. Ezrin expression in stromal cells of capillary hemangioblastoma. An immunohistochemical survey of brain tumors. Am J Pathol 1996; 148: 367-73.
    • (1996) Am J Pathol , vol.148 , pp. 367-373
    • Bohling, T.1    Turunen, O.2    Jaaskelainen, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.