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Volumn 296, Issue 2, 2004, Pages 208-222

Nuclear ERM (ezrin, radixin, moesin) proteins: Regulation by cell density and nuclear import

Author keywords

Cytoskeleton; ERM proteins; MDCK cells; Nuclear

Indexed keywords

DOMESIN; EZRIN; INSECT PROTEIN; MOESIN; NUCLEAR PROTEIN; RADIXIN; UNCLASSIFIED DRUG;

EID: 2442513975     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.02.010     Document Type: Article
Times cited : (50)

References (55)
  • 1
    • 0037448434 scopus 로고    scopus 로고
    • Cell adhesion molecule regulation of nucleocytoplasmic trafficking
    • Aplin A.E. Cell adhesion molecule regulation of nucleocytoplasmic trafficking. FEBS Lett. 534:2003;11-14
    • (2003) FEBS Lett. , vol.534 , pp. 11-14
    • Aplin, A.E.1
  • 2
    • 0031846441 scopus 로고    scopus 로고
    • Functional association of nuclear protein 4.1 with pre-mRNA splicing factors
    • Lallena M.J., Martinez C., Valcarcel J., Correas I. Functional association of nuclear protein 4.1 with pre-mRNA splicing factors. J. Cell Sci. 111:1998;1963-1971
    • (1998) J. Cell Sci. , vol.111 , pp. 1963-1971
    • Lallena, M.J.1    Martinez, C.2    Valcarcel, J.3    Correas, I.4
  • 3
    • 0036343646 scopus 로고    scopus 로고
    • Nuclear localization of the tight junction protein ZO-2 in epithelial cells
    • Islas S., Vega J., Ponce L., Gonzalez-Mariscal L. Nuclear localization of the tight junction protein ZO-2 in epithelial cells. Exp. Cell Res. 274:2002;138-148
    • (2002) Exp. Cell Res. , vol.274 , pp. 138-148
    • Islas, S.1    Vega, J.2    Ponce, L.3    Gonzalez-Mariscal, L.4
  • 6
    • 0034232066 scopus 로고    scopus 로고
    • Curbing the nuclear activities of β-catenin
    • Hecht A., Kemler R. Curbing the nuclear activities of β-catenin. EMBO Rep. 1:2000;24-28
    • (2000) EMBO Rep. , vol.1 , pp. 24-28
    • Hecht, A.1    Kemler, R.2
  • 7
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • Balda M.S., Matter K. The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. EMBO J. 19:2000;2024-2033
    • (2000) EMBO J. , vol.19 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 9
    • 0037022632 scopus 로고    scopus 로고
    • Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex
    • Rando O.J., Zhao K., Janmey P., Crabtree G.R. Phosphatidylinositol- dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex. Proc. Natl. Acad. Sci. U. S. A. 99:2002;2824-2829
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 2824-2829
    • Rando, O.J.1    Zhao, K.2    Janmey, P.3    Crabtree, G.R.4
  • 11
    • 0031842160 scopus 로고    scopus 로고
    • Analysis of molecular domains of epitope-tagged merlin isoforms in Cos-7 cells and primary rat Schwann cells
    • Xu L., Gonzalez-Agosti C., Beauchamp R., Pinney D., Sterner C., Ramesh V. Analysis of molecular domains of epitope-tagged merlin isoforms in Cos-7 cells and primary rat Schwann cells. Exp. Cell Res. 238:1998;231-240
    • (1998) Exp. Cell Res. , vol.238 , pp. 231-240
    • Xu, L.1    Gonzalez-Agosti, C.2    Beauchamp, R.3    Pinney, D.4    Sterner, C.5    Ramesh, V.6
  • 12
    • 0037106319 scopus 로고    scopus 로고
    • Nucleocytoplasmic transfer of the NF2 tumor suppressor protein merlin is regulated by exon 2 and a CRM1-dependent nuclear export signal in exon 15
    • Kressel M., Schmucker B. Nucleocytoplasmic transfer of the NF2 tumor suppressor protein merlin is regulated by exon 2 and a CRM1-dependent nuclear export signal in exon 15. Hum. Mol. Genet. 11:2002;2269-2278
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2269-2278
    • Kressel, M.1    Schmucker, B.2
  • 13
    • 0032536820 scopus 로고    scopus 로고
    • Nuclear export of actin: A novel mechanism regulating the subcellular localization of a major cytoskeletal proteins
    • Wada A., Fukuda M., Mishima M., Nishida E. Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal proteins. EMBO J. 17:1998;1635-1641
    • (1998) EMBO J. , vol.17 , pp. 1635-1641
    • Wada, A.1    Fukuda, M.2    Mishima, M.3    Nishida, E.4
  • 16
    • 0034722326 scopus 로고    scopus 로고
    • Mutagenesis of the phosphatidylinositol 4,5-bisphosphate (PIP2) binding site in the NH2-terminal domain of ezrin correlates with its altered cellular distribution
    • Barret C., Roy C., Montcourrier P., Mangeat P., Niggli V. Mutagenesis of the phosphatidylinositol 4, 5-bisphosphate (PIP2) binding site in the NH2-terminal domain of ezrin correlates with its altered cellular distribution. J. Cell Biol. 151:2000;1067-1079
    • (2000) J. Cell Biol. , vol.151 , pp. 1067-1079
    • Barret, C.1    Roy, C.2    Montcourrier, P.3    Mangeat, P.4    Niggli, V.5
  • 17
    • 0033542725 scopus 로고    scopus 로고
    • Identification of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus
    • Kaul S.C., Kawai R., Nomura H., Mitsui Y., Reddel R.R., Wadhwa R. Identification of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus. Exp. Cell Res. 250:1999;51-61
    • (1999) Exp. Cell Res. , vol.250 , pp. 51-61
    • Kaul, S.C.1    Kawai, R.2    Nomura, H.3    Mitsui, Y.4    Reddel, R.R.5    Wadhwa, R.6
  • 18
    • 0035882269 scopus 로고    scopus 로고
    • Identification of nuclei associated proteins by 2D-gel electrophoresis and mass spectrometry
    • Bergquist J., Gobom J., Blomberg A., Roepstorff P., Ekman R. Identification of nuclei associated proteins by 2D-gel electrophoresis and mass spectrometry. J. Neurosci. Methods. 109:2001;3-11
    • (2001) J. Neurosci. Methods , vol.109 , pp. 3-11
    • Bergquist, J.1    Gobom, J.2    Blomberg, A.3    Roepstorff, P.4    Ekman, R.5
  • 19
    • 0027393093 scopus 로고
    • Ezrin contains cytoskeleton and membrane-binding domains accounting for its proposed role as a membrane-cytoskeletal linker
    • Algrain M., Turunen O., Vaheri A., Louvard D., Arpin M. Ezrin contains cytoskeleton and membrane-binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J. Cell Biol. 120:1993;129-139
    • (1993) J. Cell Biol. , vol.120 , pp. 129-139
    • Algrain, M.1    Turunen, O.2    Vaheri, A.3    Louvard, D.4    Arpin, M.5
  • 20
    • 0034978943 scopus 로고    scopus 로고
    • Cellular distributions of the ERM proteins in MDCK epithelial cells: Regulation by growth and cytoskeletal integrity
    • Woodward A.M., Crouch D.H. Cellular distributions of the ERM proteins in MDCK epithelial cells: regulation by growth and cytoskeletal integrity. Cell Biol. Int. 25:2001;205-213
    • (2001) Cell Biol. Int. , vol.25 , pp. 205-213
    • Woodward, A.M.1    Crouch, D.H.2
  • 22
    • 0037413625 scopus 로고    scopus 로고
    • Moesin functions antagonistically to the Rho pathway to maintain epithelial integrity
    • Speck O., Hughes S.C., Noren N.K., Kulikauskas R.M., Fehon R.G. Moesin functions antagonistically to the Rho pathway to maintain epithelial integrity. Nature. 421:2003;83-87
    • (2003) Nature , vol.421 , pp. 83-87
    • Speck, O.1    Hughes, S.C.2    Noren, N.K.3    Kulikauskas, R.M.4    Fehon, R.G.5
  • 23
    • 0037009077 scopus 로고    scopus 로고
    • Drosophila EB1 is important for proper assembly, dynamics, and positioning of the mitotic spindle
    • Rogers S.L., Rogers G.C., Sharp D.J., Vale R.D. Drosophila EB1 is important for proper assembly, dynamics, and positioning of the mitotic spindle. J. Cell Biol. 158:2002;873-884
    • (2002) J. Cell Biol. , vol.158 , pp. 873-884
    • Rogers, S.L.1    Rogers, G.C.2    Sharp, D.J.3    Vale, R.D.4
  • 25
    • 0031240066 scopus 로고    scopus 로고
    • Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts
    • Lamb R.F., Ozanne B.W., Roy C., McGarry L., Stipp C., Mangeat P., Jay D.G. Essential functions of ezrin in maintenance of cell shape and lamellipodial extension in normal and transformed fibroblasts. Curr. Biol. 7:1997;682-688
    • (1997) Curr. Biol. , vol.7 , pp. 682-688
    • Lamb, R.F.1    Ozanne, B.W.2    Roy, C.3    McGarry, L.4    Stipp, C.5    Mangeat, P.6    Jay, D.G.7
  • 26
    • 0034631843 scopus 로고    scopus 로고
    • Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane
    • Gautreau A., Louvard D., Arpin M. Morphogenic effects of ezrin require a phosphorylation-induced transition from oligomers to monomers at the plasma membrane. J. Cell Biol. 150:2000;193-203
    • (2000) J. Cell Biol. , vol.150 , pp. 193-203
    • Gautreau, A.1    Louvard, D.2    Arpin, M.3
  • 27
    • 0029744106 scopus 로고    scopus 로고
    • The junction-associated protein, zonula occludens-1, localizes to the nucleus before maturation and during remodeling of cell-cell contacts
    • Gottardi C.J., Arpin M., Fanning A.S., Louvard D. The junction-associated protein, zonula occludens-1, localizes to the nucleus before maturation and during remodeling of cell-cell contacts. Proc. Natl. Acad. Sci. U. S. A. 93:1996;10779-10784
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 10779-10784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4
  • 29
    • 0038392934 scopus 로고    scopus 로고
    • Increased ezrin expression and activation of CDK5 coincident with acquisition of the senescent phenotype
    • Yang H.-S., Hinds P.W. Increased ezrin expression and activation of CDK5 coincident with acquisition of the senescent phenotype. Mol. Cell. 11:2003;1163-1176
    • (2003) Mol. Cell , vol.11 , pp. 1163-1176
    • Yang, H.-S.1    Hinds, P.W.2
  • 30
    • 0036797220 scopus 로고    scopus 로고
    • Dmoesin controls actin-based cell shape and polarity during Drosophila melanogaster oogenesis
    • Polesello C., Delon I., Valenti P., Ferrer P., Payre F. Dmoesin controls actin-based cell shape and polarity during Drosophila melanogaster oogenesis. Nat. Cell Biol. 4:2002;782-789
    • (2002) Nat. Cell Biol. , vol.4 , pp. 782-789
    • Polesello, C.1    Delon, I.2    Valenti, P.3    Ferrer, P.4    Payre, F.5
  • 31
    • 0141433278 scopus 로고    scopus 로고
    • Molecular requirements of actin-based lamella formation in Drosophila S2 cells
    • Rogers S.L., Wiedemann U., Stuurman N., Vale R.D. Molecular requirements of actin-based lamella formation in Drosophila S2 cells. J. Cell Biol. 162:2003;1079-1088
    • (2003) J. Cell Biol. , vol.162 , pp. 1079-1088
    • Rogers, S.L.1    Wiedemann, U.2    Stuurman, N.3    Vale, R.D.4
  • 32
    • 0032567361 scopus 로고    scopus 로고
    • Phosphorylation of moesin by Rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures
    • Oshiro N., Fukata Y., Kaibuchi K. Phosphorylation of moesin by Rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microvilli-like structures. J. Biol. Chem. 273:1998;34663-34666
    • (1998) J. Biol. Chem. , vol.273 , pp. 34663-34666
    • Oshiro, N.1    Fukata, Y.2    Kaibuchi, K.3
  • 34
    • 0242382635 scopus 로고    scopus 로고
    • Regulation of p120-catenin nucleocytoplasmic shuttling activity
    • Roczniak-Ferguson A., Reynolds A.B. Regulation of p120-catenin nucleocytoplasmic shuttling activity. J. Cell Sci. 116:2003;4201-4212
    • (2003) J. Cell Sci. , vol.116 , pp. 4201-4212
    • Roczniak-Ferguson, A.1    Reynolds, A.B.2
  • 36
    • 0035958696 scopus 로고    scopus 로고
    • Structural conversion between open and closed forms of radixin: Low-angle shadowing electron microscopy
    • Ishikawa H., Tamura A., Matsui T., Sasaki H., Hakoshima T., Tsukita S. Structural conversion between open and closed forms of radixin: low-angle shadowing electron microscopy. J. Mol. Biol. 310:2001;973-978
    • (2001) J. Mol. Biol. , vol.310 , pp. 973-978
    • Ishikawa, H.1    Tamura, A.2    Matsui, T.3    Sasaki, H.4    Hakoshima, T.5    Tsukita, S.6
  • 37
    • 0037096169 scopus 로고    scopus 로고
    • Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: An essential role for polyphosphoinositides in vivo
    • Yonemura S., Matsui T., Tsukita S., Tsukita S. Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo. J. Cell Sci. 115:2002;2569-2580
    • (2002) J. Cell Sci. , vol.115 , pp. 2569-2580
    • Yonemura, S.1    Matsui, T.2    Tsukita, S.3    Tsukita, S.4
  • 38
    • 0026760578 scopus 로고
    • Identification of the 2 major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin
    • Krieg J., Hunter T. Identification of the 2 major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin. J. Biol. Chem. 267:1992;19258-19265
    • (1992) J. Biol. Chem. , vol.267 , pp. 19258-19265
    • Krieg, J.1    Hunter, T.2
  • 39
    • 0030763919 scopus 로고    scopus 로고
    • Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cells
    • Crepaldi T., Gautreau A., Comoglio P.M., Louvard D., Arpin M. Ezrin is an effector of hepatocyte growth factor-mediated migration and morphogenesis in epithelial cells. J. Cell Biol. 138:1997;423-434
    • (1997) J. Cell Biol. , vol.138 , pp. 423-434
    • Crepaldi, T.1    Gautreau, A.2    Comoglio, P.M.3    Louvard, D.4    Arpin, M.5
  • 41
    • 0141988882 scopus 로고    scopus 로고
    • Insights into a single rod-like helix in activated radixin required for membrane-cytoskeletal cross-linking
    • Hoeflich K.P., Tsukita S., Hicks L., Kay C.M., Tsukita S., Ikura M. Insights into a single rod-like helix in activated radixin required for membrane-cytoskeletal cross-linking. Biochemistry. 42:2003;11634-11641
    • (2003) Biochemistry , vol.42 , pp. 11634-11641
    • Hoeflich, K.P.1    Tsukita, S.2    Hicks, L.3    Kay, C.M.4    Tsukita, S.5    Ikura, M.6
  • 42
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
    • Pearson M.A., Reczek D., Bretscher A., Karplus P.A. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell. 101:2000;259-270
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 43
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • Hamada K., Shimizu T., Matsui T., Tsukita S., Hakoshima T. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 19:2000;4449-4462
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, S.4    Hakoshima, T.5
  • 45
    • 0035912664 scopus 로고    scopus 로고
    • The 2.7 angstrom crystal structure of the activated FERM domain of moesin: An analysis of structural changes on activation
    • Edwards S.D., Keep N.H. The 2.7 angstrom crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation. Biochemistry. 40:2001;7061-7068
    • (2001) Biochemistry , vol.40 , pp. 7061-7068
    • Edwards, S.D.1    Keep, N.H.2
  • 46
    • 0037713484 scopus 로고    scopus 로고
    • An alternative domain containing a leucine-rich sequence regulates nuclear cytoplasmic localization of Protein 4.1R
    • Luque C.M., Perez-Ferreiro C.M., Perez-Gonzalez A., Englmeier L., Koffa M.D., Correas I. An alternative domain containing a leucine-rich sequence regulates nuclear cytoplasmic localization of Protein 4.1R. J. Biol. Chem. 278:2003;2686-2691
    • (2003) J. Biol. Chem. , vol.278 , pp. 2686-2691
    • Luque, C.M.1    Perez-Ferreiro, C.M.2    Perez-Gonzalez, A.3    Englmeier, L.4    Koffa, M.D.5    Correas, I.6
  • 47
    • 0242641546 scopus 로고    scopus 로고
    • Exportin 6: A novel nuclear export receptor that is specific for profilin:actin complexes
    • Stuven T., Hartmann E., Gorlich D. Exportin 6: a novel nuclear export receptor that is specific for profilin:actin complexes. EMBO J. 22:2003;5928-5940
    • (2003) EMBO J. , vol.22 , pp. 5928-5940
    • Stuven, T.1    Hartmann, E.2    Gorlich, D.3
  • 48
    • 0034282097 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of APC regulates β-catenin subcellular localization and turnover
    • Henderson B. Nuclear-cytoplasmic shuttling of APC regulates β-catenin subcellular localization and turnover. Nat. Cell Biol. 2:2000;653-660
    • (2000) Nat. Cell Biol. , vol.2 , pp. 653-660
    • Henderson, B.1
  • 49
    • 0037415643 scopus 로고    scopus 로고
    • The ZO-1 associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density
    • Balda M.S., Garrett M.D., Matter K. The ZO-1 associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density. J. Cell Biol. 160:2003;423-432
    • (2003) J. Cell Biol. , vol.160 , pp. 423-432
    • Balda, M.S.1    Garrett, M.D.2    Matter, K.3
  • 50
    • 0037154212 scopus 로고    scopus 로고
    • Supervillin associates with androgen receptor and modulates its transcriptional activity
    • Ting H.-J., Yeh S., Nishimura K., Chang C. Supervillin associates with androgen receptor and modulates its transcriptional activity. Proc. Natl. Acad. Sci. U. S. A. 99:2002;661-666
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 661-666
    • Ting, H.-J.1    Yeh, S.2    Nishimura, K.3    Chang, C.4
  • 51
    • 0035171968 scopus 로고    scopus 로고
    • Interaction of zyxin, a focal adhesion protein, with the E6 protein from human papillomavirus type 6 results in its nuclear translocation
    • Yan Degenhardt Y., Silverstein S. Interaction of zyxin, a focal adhesion protein, with the E6 protein from human papillomavirus type 6 results in its nuclear translocation. J. Virol. 75:2001;11791-11802
    • (2001) J. Virol. , vol.75 , pp. 11791-11802
    • Yan Degenhardt, Y.1    Silverstein, S.2
  • 52
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell-surface glycoprotein CD44 and actin-based cytoskeleton
    • Tsukita S., Oishi K., Sato N., Sagara J., Kawai A. ERM family members as molecular linkers between the cell-surface glycoprotein CD44 and actin-based cytoskeleton. J. Cell Biol. 126:1994;391-401
    • (1994) J. Cell Biol. , vol.126 , pp. 391-401
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5
  • 53
    • 0032482323 scopus 로고    scopus 로고
    • Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44
    • Legg J.W., Isacke C.M. Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44. Curr. Biol. 8:1998;705-708
    • (1998) Curr. Biol. , vol.8 , pp. 705-708
    • Legg, J.W.1    Isacke, C.M.2
  • 54
    • 0030835761 scopus 로고    scopus 로고
    • A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding
    • Roy C., Martin M., Mangeat P. A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding. J. Biol. Chem. 272:1997;20088-20095
    • (1997) J. Biol. Chem. , vol.272 , pp. 20088-20095
    • Roy, C.1    Martin, M.2    Mangeat, P.3
  • 55
    • 0035889083 scopus 로고    scopus 로고
    • Regulation of nucleocytoplasmic trafficking by cell adhesion receptors and the cytoskeleton
    • Aplin A.E., Juliano R.L. Regulation of nucleocytoplasmic trafficking by cell adhesion receptors and the cytoskeleton. J. Cell Biol. 155:2001;187-191
    • (2001) J. Cell Biol. , vol.155 , pp. 187-191
    • Aplin, A.E.1    Juliano, R.L.2


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