메뉴 건너뛰기




Volumn 421, Issue 6918, 2003, Pages 83-87

Moesin functions antagonistically to the Rho pathway to maintain epithelial integrity

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; MEMBRANES; PROTEINS;

EID: 0037413625     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01295     Document Type: Article
Times cited : (215)

References (30)
  • 1
    • 0035674837 scopus 로고    scopus 로고
    • Epithelial cell polarity and cell junctions in Drosophila
    • Tepass, U., Tanentzapf, G., Ward, R. & Fehon, R. Epithelial cell polarity and cell junctions in Drosophila. Annu. Rev. Genet. 35, 747-784 (2001).
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 747-784
    • Tepass, U.1    Tanentzapf, G.2    Ward, R.3    Fehon, R.4
  • 2
    • 0035818984 scopus 로고    scopus 로고
    • Drosophila Stardust is a partner of Crumbs in the control of epithelial cell polarity
    • Bachmann, A., Schneider, M., Theilenberg, E., Grawe, P. & Knust, E. Drosophila Stardust is a partner of Crumbs in the control of epithelial cell polarity. Nature 414, 638-643 (2001).
    • (2001) Nature , vol.414 , pp. 638-643
    • Bachmann, A.1    Schneider, M.2    Theilenberg, E.3    Grawe, P.4    Knust, E.5
  • 3
    • 0034785272 scopus 로고    scopus 로고
    • Spatial control of the actin cytoskeleton in Drosophila epithelial cells
    • Baum, B. & Perrimon, N. Spatial control of the actin cytoskeleton in Drosophila epithelial cells. Nature Cell Biol. 3, 883-890 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 883-890
    • Baum, B.1    Perrimon, N.2
  • 4
    • 0031471375 scopus 로고    scopus 로고
    • Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures
    • Bretscher, A., Reczek, D. & Berryman, M. Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J. Cell Sci. 110, 3011-3018 (1997).
    • (1997) J. Cell Sci. , vol.110 , pp. 3011-3018
    • Bretscher, A.1    Reczek, D.2    Berryman, M.3
  • 6
    • 0034708480 scopus 로고    scopus 로고
    • The genome sequence of Drosophila melanogaster
    • Adams, M. D. et al. The genome sequence of Drosophila melanogaster. Science 287, 2185-2195 (2000).
    • (2000) Science , vol.287 , pp. 2185-2195
    • Adams, M.D.1
  • 7
    • 0029945453 scopus 로고    scopus 로고
    • Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumour suppressor, merlin
    • McCartney, B. M. & Fehon, R. G. Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumour suppressor, merlin. J. Cell Biol. 133, 843-852 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 843-852
    • McCartney, B.M.1    Fehon, R.G.2
  • 8
    • 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. et al. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J. Cell Biol. 140, 647-657 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 647-657
    • Matsui, T.1
  • 9
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
    • Shaw, R. J., Henry, M., Solomon, F. & Jacks, T. RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. Mol. Biol. Cell 9, 403-419 (1998).
    • (1998) Mol. Biol. Cell , vol.9 , pp. 403-419
    • Shaw, R.J.1    Henry, M.2    Solomon, F.3    Jacks, T.4
  • 10
    • 0032583447 scopus 로고    scopus 로고
    • C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton
    • Simons, P. C., Pietromonaco, S. F., Reczek, D., Bretscher, A. & Elias, L. C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical lipid bilayer to the cytoskeleton. Biochem. Biophys. Res. Commun. 253, 561-565 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 561-565
    • Simons, P.C.1    Pietromonaco, S.F.2    Reczek, D.3    Bretscher, A.4    Elias, L.5
  • 11
    • 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. Nature Cell Biol. 4, 782-789 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 782-789
    • Polesello, C.1    Delon, I.2    Valenti, P.3    Ferrer, P.4    Payre, F.5
  • 12
    • 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, 193-203 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 193-203
    • Gautreau, A.1    Louvard, D.2    Arpin, M.3
  • 14
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao, M. et al. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J. Cell Biol. 135, 37-51 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 37-51
    • Hirao, M.1
  • 15
    • 0030872949 scopus 로고    scopus 로고
    • Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • Mackay, D. J., Esch, F., Furthmayr, H. & Hall, A. Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. J. Cell Biol. 138, 927-938 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 927-938
    • Mackay, D.J.1    Esch, F.2    Furthmayr, H.3    Hall, A.4
  • 16
    • 0030917227 scopus 로고    scopus 로고
    • The role of RhoA in tissue polarity and Frizzled signalling
    • Strutt, D. I., Weber, U. & Mlodzik, M. The role of RhoA in tissue polarity and Frizzled signalling. Nature 387, 292-295 (1997).
    • (1997) Nature , vol.387 , pp. 292-295
    • Strutt, D.I.1    Weber, U.2    Mlodzik, M.3
  • 17
    • 0035815280 scopus 로고    scopus 로고
    • Drosophila Rho-associated kinase (Drok) links Frizzled-mediated planar cell polarity signaling to the actin cytoskeleton
    • Winter, C. G. et al. Drosophila Rho-associated kinase (Drok) links Frizzled-mediated planar cell polarity signaling to the actin cytoskeleton. Cell 105, 81-91 (2001).
    • (2001) Cell , vol.105 , pp. 81-91
    • Winter, C.G.1
  • 18
    • 0033832543 scopus 로고    scopus 로고
    • Genetic analysis demonstrates a direct link between rho signaling and nonmuscle myosin function during Drosophila morphogenesis
    • Halsell, S. R., Chu, B. I. & Kiehart, D. P. Genetic analysis demonstrates a direct link between rho signaling and nonmuscle myosin function during Drosophila morphogenesis. Genetics 156, 469 (2000).
    • (2000) Genetics , vol.156 , pp. 469
    • Halsell, S.R.1    Chu, B.I.2    Kiehart, D.P.3
  • 19
    • 0032950502 scopus 로고    scopus 로고
    • Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues
    • Hayashi, K., Yonemura, S., Matsui, T. & Tsukita, S. Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues. J. Cell Sci. 112, 1149-1158 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 1149-1158
    • Hayashi, K.1    Yonemura, S.2    Matsui, T.3    Tsukita, S.4
  • 20
    • 0031281917 scopus 로고    scopus 로고
    • GFP-moesin illuminates actin cytoskeleton dynamics in living tissue and demonstrates cell shape changes during morphogenesis in Drosophila
    • Edwards, K. A., Demsky, M., Montague, R. A., Weymouth, N. & Kiehart, D. P. GFP-moesin illuminates actin cytoskeleton dynamics in living tissue and demonstrates cell shape changes during morphogenesis in Drosophila. Dev. Biol. 191, 103-117 (1997).
    • (1997) Dev. Biol. , vol.191 , pp. 103-117
    • Edwards, K.A.1    Demsky, M.2    Montague, R.A.3    Weymouth, N.4    Kiehart, D.P.5
  • 21
    • 0030846295 scopus 로고    scopus 로고
    • Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
    • Takahashi, K. et al. Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J. Biol. Chem. 272, 23371-23375 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23371-23375
    • Takahashi, K.1
  • 22
    • 0032566011 scopus 로고    scopus 로고
    • Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl
    • Takahashi, K. et al. Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl. Oncogene 16, 3279-3284 (1998).
    • (1998) Oncogene , vol.16 , pp. 3279-3284
    • Takahashi, K.1
  • 23
    • 18044399847 scopus 로고    scopus 로고
    • The Nf2 tumour suppressor, merlin, functions in Rac-dependent signaling
    • Shaw, R. J. et al. The Nf2 tumour suppressor, merlin, functions in Rac-dependent signaling. Dev. Cell 1, 63-72 (2001).
    • (2001) Dev. Cell , vol.1 , pp. 63-72
    • Shaw, R.J.1
  • 24
    • 0032578033 scopus 로고    scopus 로고
    • Structural analysis of Drosophila merlin reveals functional domains important for growth control and subcellular localization
    • LaJeunesse, D. R., McCartney, B. M. & Fehon, R. G. Structural analysis of Drosophila merlin reveals functional domains important for growth control and subcellular localization. J. Cell Biol. 141, 1589-1599 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 1589-1599
    • LaJeunesse, D.R.1    McCartney, B.M.2    Fehon, R.G.3
  • 25
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A. H. & Perrimon, N. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118, 401-415 (1993).
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 26
    • 0027306001 scopus 로고
    • Specific truncations of Drosophila Notch define dominant activated and dominant negative forms of the receptor
    • Rebay, I., Fehon, R. G. & Artavanis-Tsakonas, S. Specific truncations of Drosophila Notch define dominant activated and dominant negative forms of the receptor. Cell 74, 319-329 (1993).
    • (1993) Cell , vol.74 , pp. 319-329
    • Rebay, I.1    Fehon, R.G.2    Artavanis-Tsakonas, S.3
  • 27
    • 0028325048 scopus 로고
    • A Drosophila homologue of membrane-skeleton protein 4.1 is associated with septate junctions and is encoded by the coracle gene
    • Fehon, R. G., Dawson, I. A. & Artavanis-Tsakonas, S. A Drosophila homologue of membrane-skeleton protein 4.1 is associated with septate junctions and is encoded by the coracle gene. Development 120, 545-557 (1994).
    • (1994) Development , vol.120 , pp. 545-557
    • Fehon, R.G.1    Dawson, I.A.2    Artavanis-Tsakonas, S.3
  • 28
    • 0030273675 scopus 로고    scopus 로고
    • Presynaptic development at the Drosophila neuromuscular junction: Assembly and localization of presynaptic active zones
    • Prokop, A., Landgraf, M., Rushton, E., Broadie, K. & Bate, M. Presynaptic development at the Drosophila neuromuscular junction: assembly and localization of presynaptic active zones. Neuron 17, 617-626 (1996).
    • (1996) Neuron , vol.17 , pp. 617-626
    • Prokop, A.1    Landgraf, M.2    Rushton, E.3    Broadie, K.4    Bate, M.5
  • 29
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X. D., Kiosses, W. B. & Schwartz, M. A. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18, 578-585 (1999).
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 30
    • 0034618050 scopus 로고    scopus 로고
    • p120 catenin regulates the actin cytoskeleton via Rho family GTPases
    • Noren, N. K., Liu, B. P., Burridge, K. & Kreft, B. p120 catenin regulates the actin cytoskeleton via Rho family GTPases. J. Cell Biol. 150, 567-580 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 567-580
    • Noren, N.K.1    Liu, B.P.2    Burridge, K.3    Kreft, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.