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Volumn 305, Issue 1, 2005, Pages 74-82

Rnd3/RhoE induces tight junction formation in mammary epithelial tumor cells

Author keywords

Apical junctional complex; RhoA; Rnd3 RhoE; Small GTPases; Tight junctions

Indexed keywords

ACTIN; BETA CATENIN; GLUCOCORTICOID; GUANOSINE TRIPHOSPHATASE RHO E; PROTEIN ZO1; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 15044361337     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.12.010     Document Type: Article
Times cited : (19)

References (54)
  • 1
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • B.M. Gumbiner Cell adhesion: the molecular basis of tissue architecture and morphogenesis Cell 84 1996 345 357
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 2
    • 0031943571 scopus 로고    scopus 로고
    • Regulation of the movement of solutes across tight junctions
    • J.L. Madara Regulation of the movement of solutes across tight junctions Annu. Rev. Physiol. 60 1998 143 159
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 143-159
    • Madara, J.L.1
  • 3
    • 0023612699 scopus 로고
    • Structure, biochemistry, and assembly of epithelial tight junctions
    • B. Gumbiner Structure, biochemistry, and assembly of epithelial tight junctions Am. J. Physiol. 253 1987 C749 C758
    • (1987) Am. J. Physiol. , vol.253
    • Gumbiner, B.1
  • 4
  • 6
    • 0022516245 scopus 로고
    • The tight junction does not allow lipid molecules to diffuse from one epithelial cell to the next
    • G. van Meer, B. Gumbiner, and K. Simons The tight junction does not allow lipid molecules to diffuse from one epithelial cell to the next Nature 322 1986 639 641
    • (1986) Nature , vol.322 , pp. 639-641
    • Van Meer, G.1    Gumbiner, B.2    Simons, K.3
  • 7
    • 0035479827 scopus 로고    scopus 로고
    • Molecular architecture of adherens junctions
    • A. Nagafuchi Molecular architecture of adherens junctions Curr. Opin. Cell Biol. 13 2001 600 603
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 600-603
    • Nagafuchi, A.1
  • 8
    • 0037459077 scopus 로고    scopus 로고
    • Sticky business: Orchestrating cellular signals at adherens junctions
    • M. Perez-Moreno, C. Jamora, and E. Fuchs Sticky business: orchestrating cellular signals at adherens junctions Cell 112 2003 535 548
    • (2003) Cell , vol.112 , pp. 535-548
    • Perez-Moreno, M.1    Jamora, C.2    Fuchs, E.3
  • 9
    • 0028979956 scopus 로고
    • Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin
    • K.A. Knudsen, A.P. Soler, K.R. Johnson, and M.J. Wheelock Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin J. Cell Biol. 130 1995 67 77
    • (1995) J. Cell Biol. , vol.130 , pp. 67-77
    • Knudsen, K.A.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 10
    • 0030926845 scopus 로고    scopus 로고
    • Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin
    • J.E. Nieset, A.R. Redfield, F. Jin, K.A. Knudsen, K.R. Johnson, and M.J. Wheelock Characterization of the interactions of alpha-catenin with alpha-actinin and beta-catenin/plakoglobin J. Cell Sci. 110 Pt 8 1997 1013 1022
    • (1997) J. Cell Sci. , vol.110 , Issue.8 PART , pp. 1013-1022
    • Nieset, J.E.1    Redfield, A.R.2    Jin, F.3    Knudsen, K.A.4    Johnson, K.R.5    Wheelock, M.J.6
  • 11
    • 0027207967 scopus 로고
    • The molecular organization of tight junctions
    • S. Citi The molecular organization of tight junctions J. Cell Biol. 121 1993 485 489
    • (1993) J. Cell Biol. , vol.121 , pp. 485-489
    • Citi, S.1
  • 12
    • 0038617335 scopus 로고    scopus 로고
    • Functional analysis of tight junctions
    • K. Matter, and M.S. Balda Functional analysis of tight junctions Methods 30 2003 228 234
    • (2003) Methods , vol.30 , pp. 228-234
    • Matter, K.1    Balda, M.S.2
  • 13
    • 0028850390 scopus 로고
    • Glucocorticoid-induced functional polarity of growth factor responsiveness regulates tight junction dynamics in transformed mammary epithelial tumor cells
    • P. Buse, P.L. Woo, D.B. Alexander, A. Reza, and G.L. Firestone Glucocorticoid-induced functional polarity of growth factor responsiveness regulates tight junction dynamics in transformed mammary epithelial tumor cells J. Biol. Chem. 270 1995 28223 28227
    • (1995) J. Biol. Chem. , vol.270 , pp. 28223-28227
    • Buse, P.1    Woo, P.L.2    Alexander, D.B.3    Reza, A.4    Firestone, G.L.5
  • 14
    • 0033605134 scopus 로고    scopus 로고
    • Glucocorticoid down-regulation of fascin protein expression is required for the steroid-induced formation of tight junctions and cell-cell interactions in rat mammary epithelial tumor cells
    • V. Wong, D. Ching, P.D. McCrea, and G.L. Firestone Glucocorticoid down-regulation of fascin protein expression is required for the steroid-induced formation of tight junctions and cell-cell interactions in rat mammary epithelial tumor cells J. Biol. Chem. 274 1999 5443 5453
    • (1999) J. Biol. Chem. , vol.274 , pp. 5443-5453
    • Wong, V.1    Ching, D.2    McCrea, P.D.3    Firestone, G.L.4
  • 15
    • 0034666304 scopus 로고    scopus 로고
    • Involvement of the helix-loop-helix protein Id-1 in the glucocorticoid regulation of tight junctions in mammary epithelial cells
    • P.L. Woo, A. Cercek, P.Y. Desprez, and G.L. Firestone Involvement of the helix-loop-helix protein Id-1 in the glucocorticoid regulation of tight junctions in mammary epithelial cells J. Biol. Chem. 275 2000 28649 28658
    • (2000) J. Biol. Chem. , vol.275 , pp. 28649-28658
    • Woo, P.L.1    Cercek, A.2    Desprez, P.Y.3    Firestone, G.L.4
  • 16
    • 0032752371 scopus 로고    scopus 로고
    • Requirement for Ras and phosphatidylinositol 3-kinase signaling uncouples the glucocorticoid-induced junctional organization and transepithelial electrical resistance in mammary tumor cells
    • P.L. Woo, D. Ching, Y. Guan, and G.L. Firestone Requirement for Ras and phosphatidylinositol 3-kinase signaling uncouples the glucocorticoid-induced junctional organization and transepithelial electrical resistance in mammary tumor cells J. Biol. Chem. 274 1999 32818 32828
    • (1999) J. Biol. Chem. , vol.274 , pp. 32818-32828
    • Woo, P.L.1    Ching, D.2    Guan, Y.3    Firestone, G.L.4
  • 17
    • 0037456847 scopus 로고    scopus 로고
    • Links between signal transduction, transcription and adhesion in epithelial bud development
    • C. Jamora, R. DasGupta, P. Kocieniewski, and E. Fuchs Links between signal transduction, transcription and adhesion in epithelial bud development Nature 422 2003 317 322
    • (2003) Nature , vol.422 , pp. 317-322
    • Jamora, C.1    Dasgupta, R.2    Kocieniewski, P.3    Fuchs, E.4
  • 19
    • 0036774217 scopus 로고    scopus 로고
    • Cell-cell adhesion and signalling
    • V.M. Braga Cell-cell adhesion and signalling Curr. Opin. Cell Biol. 14 2002 546 556
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 546-556
    • Braga, V.M.1
  • 20
    • 0032514214 scopus 로고    scopus 로고
    • Effects of regulated expression of mutant RhoA and Rac1 small GTPases on the development of epithelial (MDCK) cell polarity
    • T.S. Jou, and W.J. Nelson Effects of regulated expression of mutant RhoA and Rac1 small GTPases on the development of epithelial (MDCK) cell polarity J. Cell Biol. 142 1998 85 100
    • (1998) J. Cell Biol. , vol.142 , pp. 85-100
    • Jou, T.S.1    Nelson, W.J.2
  • 21
    • 0032514134 scopus 로고    scopus 로고
    • Structural and functional regulation of tight junctions by RhoA and Rac1 small GTPases
    • T.S. Jou, E.E. Schneeberger, and W.J. Nelson Structural and functional regulation of tight junctions by RhoA and Rac1 small GTPases J. Cell Biol. 142 1998 101 115
    • (1998) J. Cell Biol. , vol.142 , pp. 101-115
    • Jou, T.S.1    Schneeberger, E.E.2    Nelson, W.J.3
  • 22
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells
    • K. Takaishi, T. Sasaki, H. Kotani, H. Nishioka, and Y. Takai Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells J. Cell Biol. 139 1997 1047 1059
    • (1997) J. Cell Biol. , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 24
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • S. Etienne-Manneville, and A. Hall Rho GTPases in cell biology Nature 420 2002 629 635
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 26
    • 0038532299 scopus 로고    scopus 로고
    • Glucocorticoid down-regulation of RhoA is required for the steroid-induced organization of the junctional complex and tight junction formation in rat mammary epithelial tumor cells
    • N.M. Rubenstein, Y. Guan, P.L. Woo, and G.L. Firestone Glucocorticoid down-regulation of RhoA is required for the steroid-induced organization of the junctional complex and tight junction formation in rat mammary epithelial tumor cells J. Biol. Chem. 278 2003 10353 10360
    • (2003) J. Biol. Chem. , vol.278 , pp. 10353-10360
    • Rubenstein, N.M.1    Guan, Y.2    Woo, P.L.3    Firestone, G.L.4
  • 27
    • 0032489841 scopus 로고    scopus 로고
    • A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion
    • C.D. Nobes, I. Lauritzen, M.G. Mattei, S. Paris, A. Hall, and P. Chardin A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion J. Cell Biol. 141 1998 187 197
    • (1998) J. Cell Biol. , vol.141 , pp. 187-197
    • Nobes, C.D.1    Lauritzen, I.2    Mattei, M.G.3    Paris, S.4    Hall, A.5    Chardin, P.6
  • 30
    • 0031877714 scopus 로고    scopus 로고
    • RhoE regulates actin cytoskeleton organization and cell migration
    • R.M. Guasch, P. Scambler, G.E. Jones, and A.J. Ridley RhoE regulates actin cytoskeleton organization and cell migration Mol. Cell. Biol. 18 1998 4761 4771
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4761-4771
    • Guasch, R.M.1    Scambler, P.2    Jones, G.E.3    Ridley, A.J.4
  • 31
    • 0034461613 scopus 로고    scopus 로고
    • Induced expression of Rnd3 is associated with transformation of polarized epithelial cells by the Raf-MEK-extracellular signal-regulated kinase pathway
    • S.H. Hansen, M.M. Zegers, M. Woodrow, P. Rodriguez-Viciana, P. Chardin, K.E. Mostov, and M. McMahon Induced expression of Rnd3 is associated with transformation of polarized epithelial cells by the Raf-MEK-extracellular signal-regulated kinase pathway Mol. Cell. Biol. 20 2000 9364 9375
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 9364-9375
    • Hansen, S.H.1    Zegers, M.M.2    Woodrow, M.3    Rodriguez-Viciana, P.4    Chardin, P.5    Mostov, K.E.6    McMahon, M.7
  • 32
    • 4444355324 scopus 로고    scopus 로고
    • RhoE inhibits cell cycle progression and Ras-induced transformation
    • P. Villalonga, R.M. Guasch, K. Riento, and A.J. Ridley RhoE inhibits cell cycle progression and Ras-induced transformation Mol. Cell. Biol. 24 2004 7829 7840
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7829-7840
    • Villalonga, P.1    Guasch, R.M.2    Riento, K.3    Ridley, A.J.4
  • 33
    • 0025237524 scopus 로고
    • Suppression of rat mammary tumor cell growth in vitro by glucocorticoids requires serum proteins. Characterization of wild type and glucocorticoid- resistant epithelial tumor cells
    • M.K. Webster, J. Guthrie, and G.L. Firestone Suppression of rat mammary tumor cell growth in vitro by glucocorticoids requires serum proteins. Characterization of wild type and glucocorticoid-resistant epithelial tumor cells J. Biol. Chem. 265 1990 4831 4838
    • (1990) J. Biol. Chem. , vol.265 , pp. 4831-4838
    • Webster, M.K.1    Guthrie, J.2    Firestone, G.L.3
  • 34
    • 0026329981 scopus 로고
    • Glucocorticoid growth suppression response in 13762NF adenocarcinoma-derived Con8 rat mammary tumor cells is mediated by dominant trans-acting factors
    • M.K. Webster, J. Guthrie, and G.L. Firestone Glucocorticoid growth suppression response in 13762NF adenocarcinoma-derived Con8 rat mammary tumor cells is mediated by dominant trans-acting factors Cancer Res. 51 1991 6031 6038
    • (1991) Cancer Res. , vol.51 , pp. 6031-6038
    • Webster, M.K.1    Guthrie, J.2    Firestone, G.L.3
  • 35
    • 0027534990 scopus 로고
    • Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum
    • M.K. Webster, L. Goya, Y. Ge, A.C. Maiyar, and G.L. Firestone Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum Mol. Cell. Biol. 13 1993 2031 2040
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2031-2040
    • Webster, M.K.1    Goya, L.2    Ge, Y.3    Maiyar, A.C.4    Firestone, G.L.5
  • 38
    • 0034823910 scopus 로고    scopus 로고
    • Rho kinase regulates tight junction function and is necessary for tight junction assembly in polarized intestinal epithelia
    • S.V. Walsh, A.M. Hopkins, J. Chen, S. Narumiya, C.A. Parkos, and A. Nusrat Rho kinase regulates tight junction function and is necessary for tight junction assembly in polarized intestinal epithelia Gastroenterology 121 2001 566 579
    • (2001) Gastroenterology , vol.121 , pp. 566-579
    • Walsh, S.V.1    Hopkins, A.M.2    Chen, J.3    Narumiya, S.4    Parkos, C.A.5    Nusrat, A.6
  • 39
    • 0036232358 scopus 로고    scopus 로고
    • Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers
    • H. Katoh, A. Harada, K. Mori, and M. Negishi Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers Mol. Cell. Biol. 22 2002 2952 2964
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2952-2964
    • Katoh, H.1    Harada, A.2    Mori, K.3    Negishi, M.4
  • 40
    • 0027500533 scopus 로고
    • The effect of posttranslational modifications on the interaction of Ras2 with adenylyl cyclase
    • Y. Kuroda, N. Suzuki, and T. Kataoka The effect of posttranslational modifications on the interaction of Ras2 with adenylyl cyclase Science 259 1993 683 686
    • (1993) Science , vol.259 , pp. 683-686
    • Kuroda, Y.1    Suzuki, N.2    Kataoka, T.3
  • 41
    • 0029894664 scopus 로고    scopus 로고
    • Identification of a novel human Rho protein with unusual properties: GTPase deficiency and in vivo farnesylation
    • R. Foster, K.Q. Hu, Y. Lu, K.M. Nolan, J. Thissen, and J. Settleman Identification of a novel human Rho protein with unusual properties: GTPase deficiency and in vivo farnesylation Mol. Cell. Biol. 16 1996 2689 2699
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2689-2699
    • Foster, R.1    Hu, K.Q.2    Lu, Y.3    Nolan, K.M.4    Thissen, J.5    Settleman, J.6
  • 42
    • 0013161392 scopus 로고    scopus 로고
    • Mechanisms of Ras protein targeting in mammalian cells
    • J.R. Silvius Mechanisms of Ras protein targeting in mammalian cells J. Membr. Biol. 190 2002 83 92
    • (2002) J. Membr. Biol. , vol.190 , pp. 83-92
    • Silvius, J.R.1
  • 43
    • 0035825193 scopus 로고    scopus 로고
    • Differential localization of Rho GTPases in live cells: Regulation by hypervariable regions and RhoGDI binding
    • D. Michaelson, J. Silletti, G. Murphy, P. D'Eustachio, M. Rush, and M.R. Philips Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding J. Cell Biol. 152 2001 111 126
    • (2001) J. Cell Biol. , vol.152 , pp. 111-126
    • Michaelson, D.1    Silletti, J.2    Murphy, G.3    D'Eustachio, P.4    Rush, M.5    Philips, M.R.6
  • 45
    • 0034695656 scopus 로고    scopus 로고
    • Directed actin polymerization is the driving force in epithelial cell-cell adhesion
    • V. Vasioukhin, C. Bauer, M. Yin, and E. Fuchs Directed actin polymerization is the driving force in epithelial cell-cell adhesion Cell 100 2000 209 219
    • (2000) Cell , vol.100 , pp. 209-219
    • Vasioukhin, V.1    Bauer, C.2    Yin, M.3    Fuchs, E.4
  • 46
    • 0032563564 scopus 로고    scopus 로고
    • Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein
    • C.L. Adams, Y.T. Chen, S.J. Smith, and W.J. Nelson Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent protein J. Cell Biol. 142 1998 1105 1119
    • (1998) J. Cell Biol. , vol.142 , pp. 1105-1119
    • Adams, C.L.1    Chen, Y.T.2    Smith, S.J.3    Nelson, W.J.4
  • 47
    • 1342310742 scopus 로고    scopus 로고
    • Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables
    • A. Kobielak, H.A. Pasolli, and E. Fuchs Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables Nat. Cell Biol. 6 2004 21 30
    • (2004) Nat. Cell Biol. , vol.6 , pp. 21-30
    • Kobielak, A.1    Pasolli, H.A.2    Fuchs, E.3
  • 48
    • 0032939619 scopus 로고    scopus 로고
    • Rho GTPases are over-expressed in human tumors
    • G. Fritz, I. Just, and B. Kaina Rho GTPases are over-expressed in human tumors Int. J. Cancer 81 1999 682 687
    • (1999) Int. J. Cancer , vol.81 , pp. 682-687
    • Fritz, G.1    Just, I.2    Kaina, B.3
  • 49
    • 0036226043 scopus 로고    scopus 로고
    • The rho/rho-kinase pathway is involved in the progression of testicular germ cell tumour
    • T. Kamai, K. Arai, S. Sumi, T. Tsujii, M. Honda, T. Yamanishi, and K.I. Yoshida The rho/rho-kinase pathway is involved in the progression of testicular germ cell tumour BJU Int. 89 2002 449 453
    • (2002) BJU Int. , vol.89 , pp. 449-453
    • Kamai, T.1    Arai, K.2    Sumi, S.3    Tsujii, T.4    Honda, M.5    Yamanishi, T.6    Yoshida, K.I.7
  • 50
    • 0035129473 scopus 로고    scopus 로고
    • Overexpression of RhoA mRNA is associated with advanced stage in testicular germ cell tumour
    • T. Kamai, K. Arai, T. Tsujii, M. Honda, and K. Yoshida Overexpression of RhoA mRNA is associated with advanced stage in testicular germ cell tumour Br. J. Urol. Iint. 87 2001 227 231
    • (2001) Br. J. Urol. Iint. , vol.87 , pp. 227-231
    • Kamai, T.1    Arai, K.2    Tsujii, T.3    Honda, M.4    Yoshida, K.5
  • 51
    • 0035874879 scopus 로고    scopus 로고
    • Inhibition of epidermal growth factor-induced RhoA translocation and invasion of human pancreatic cancer cells by 3-hydroxy-3-methylglutaryl-coenzyme a reductase inhibitors
    • T. Kusama, M. Mukai, T. Iwasaki, M. Tatsuta, Y. Matsumoto, H. Akedo, and H. Nakramura Inhibition of epidermal growth factor-induced RhoA translocation and invasion of human pancreatic cancer cells by 3-hydroxy-3-methylglutaryl- coenzyme a reductase inhibitors Cancer Res. 61 2001 4885 4891
    • (2001) Cancer Res. , vol.61 , pp. 4885-4891
    • Kusama, T.1    Mukai, M.2    Iwasaki, T.3    Tatsuta, M.4    Matsumoto, Y.5    Akedo, H.6    Nakramura, H.7
  • 52
    • 0242606225 scopus 로고    scopus 로고
    • Up-regulation of Rnd1 during pregnancy serves as a negative-feedback control for Ca2+ sensitization of contractile elements in rat myometrium
    • Y. Kim, B. Kim, H. Karaki, M. Hori, and H. Ozaki Up-regulation of Rnd1 during pregnancy serves as a negative-feedback control for Ca2+ sensitization of contractile elements in rat myometrium Biochem. Biophys. Res. Commun. 311 2003 972 978
    • (2003) Biochem. Biophys. Res. Commun. , vol.311 , pp. 972-978
    • Kim, Y.1    Kim, B.2    Karaki, H.3    Hori, M.4    Ozaki, H.5
  • 53
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: Multifunctional kinases in cell behaviour
    • K. Riento, and A.J. Ridley Rocks: multifunctional kinases in cell behaviour Nat. Rev., Mol. Cell Biol. 4 2003 446 456
    • (2003) Nat. Rev., Mol. Cell Biol. , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 54
    • 0037413625 scopus 로고    scopus 로고
    • Moesin functions antagonistically to the Rho pathway to maintain epithelial integrity
    • O. Speck, S.C. Hughes, N.K. Noren, R.M. Kulikauskas, and R.G. Fehon 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


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