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Volumn 11, Issue 5, 1999, Pages 591-596

Regulation of cadherin-mediated cell-cell adhesion by the rho family GTPases

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CATENIN; BETA CATENIN; CADHERIN; CELL ADHESION MOLECULE; GUANOSINE TRIPHOSPHATASE; RHO FACTOR;

EID: 0032859045     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)00014-9     Document Type: Review
Times cited : (170)

References (67)
  • 1
    • 0025325167 scopus 로고
    • Cadherins: A molecular family important in selective cell-cell adhesion
    • Takeichi M Cadherins: a molecular family important in selective cell-cell adhesion. Annu Rev Biochem. 59:1990;237-252.
    • (1990) Annu Rev Biochem , vol.59 , pp. 237-252
    • Takeichi, M.1
  • 2
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner BM 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
  • 3
    • 0342327346 scopus 로고    scopus 로고
    • Cadherins, catenins and APC protein: Interplay between cytoskeletal complexes and signaling pathways
    • Barth A, Nathke IS, Nelson WJ Cadherins, catenins and APC protein: interplay between cytoskeletal complexes and signaling pathways. Curr Opin Cell Biol. 9:1997;683-690.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 683-690
    • Barth, A.1    Nathke, I.S.2    Nelson, W.J.3
  • 4
    • 0024451982 scopus 로고
    • The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species
    • Ozawa M, Baribault H, Kemler R The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species. EMBO J. 8:1989;1711-1717.
    • (1989) EMBO J , vol.8 , pp. 1711-1717
    • Ozawa, M.1    Baribault, H.2    Kemler, R.3
  • 5
    • 0026940189 scopus 로고
    • Molecular linkage between cadherins and actin filaments in cell-cell adherens junctions
    • Tsukita S, Tsukita S, Nagafuchi A, Yonemura S Molecular linkage between cadherins and actin filaments in cell-cell adherens junctions. Curr Opin Cell Biol. 4:1992;834-839.
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 834-839
    • Tsukita, S.1    Tsukita, S.2    Nagafuchi, A.3    Yonemura, S.4
  • 6
    • 0031692261 scopus 로고    scopus 로고
    • Cytomechanics of cadherin-mediated cell-cell adhesion
    • Adams CL, Nelson WJ Cytomechanics of cadherin-mediated cell-cell adhesion. Curr Opin Cell Biol. 10:1998;572-577.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 572-577
    • Adams, C.L.1    Nelson, W.J.2
  • 7
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst L, D'Souza-Schorey C Rho GTPases and signaling networks. Genes Dev. 11:1997;2295-2322.
    • (1997) Genes Dev , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 8
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • This review summarises how the Rho family GTPases regulate various cellular processes, including cytoskeleton, cell adhesion and gene expression.
    • Hall A Rho GTPases and the actin cytoskeleton. Science. 279:1998;509-514. This review summarises how the Rho family GTPases regulate various cellular processes, including cytoskeleton, cell adhesion and gene expression.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 9
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 11
    • 0027471215 scopus 로고
    • Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, Rho
    • Tominaga T, Sugie K, Hirata M, Morii N, Fukata J, Uchida A, Imura H, Narumiya S Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, Rho. J Cell Biol. 120:1993;1529-1537.
    • (1993) J Cell Biol , vol.120 , pp. 1529-1537
    • Tominaga, T.1    Sugie, K.2    Hirata, M.3    Morii, N.4    Fukata, J.5    Uchida, A.6    Imura, H.7    Narumiya, S.8
  • 12
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga V, Machesky LM, Hall A, Hotchin NA The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J Cell Biol. 137:1997;1421-1431.
    • (1997) J Cell Biol , vol.137 , pp. 1421-1431
    • Braga, V.1    MacHesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 13
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells
    • Takaishi K, Sasaki T, Kotani H, Nishioka H, Takai Y 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
  • 15
    • 0028258943 scopus 로고
    • Rac p21 is involved in insulin-induced membrane ruffling and Rho p21 is involved in hepatocyte growth factor- And 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells
    • Nishiyama T, Sasaki T, Takaishi K, Kato M, Yaku H, Araki K, Matsuura Y, Takai Y Rac p21 is involved in insulin-induced membrane ruffling and Rho p21 is involved in hepatocyte growth factor- and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells. Mol Cell Biol. 14:1994;2447-2456.
    • (1994) Mol Cell Biol , vol.14 , pp. 2447-2456
    • Nishiyama, T.1    Sasaki, T.2    Takaishi, K.3    Kato, M.4    Yaku, H.5    Araki, K.6    Matsuura, Y.7    Takai, Y.8
  • 18
  • 19
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- And thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho
    • Jalink K, van Corven EJ, Hengeveld T, Morii N, Narumiya S, Moolenaar WH Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. J Cell Biol. 126:1994;801-810.
    • (1994) J Cell Biol , vol.126 , pp. 801-810
    • Jalink, K.1    Van Corven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 20
    • 0027509362 scopus 로고
    • Regulation of cytoplasmic division of Xenopus embryo by Rho p21 and its inhibitory GDP/GTP exchange protein (Rho GDI)
    • Kishi K, Sasaki T, Kuroda S, Itoh T, Takai Y Regulation of cytoplasmic division of Xenopus embryo by Rho p21 and its inhibitory GDP/GTP exchange protein (Rho GDI). J Cell Biol. 120:1993;1187-1195.
    • (1993) J Cell Biol , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 21
    • 0027691240 scopus 로고
    • A Rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs
    • Mabuchi I, Hamaguchi Y, Fujimoto H, Morii N, Mishima M, Narumiya S A Rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs. Zygote. 1:1993;325-331.
    • (1993) Zygote , vol.1 , pp. 325-331
    • Mabuchi, I.1    Hamaguchi, Y.2    Fujimoto, H.3    Morii, N.4    Mishima, M.5    Narumiya, S.6
  • 22
    • 0026654125 scopus 로고
    • The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling
    • Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling. Cell. 70:1992;401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 23
    • 0028894787 scopus 로고
    • Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells
    • Ridley AJ, Comoglio PM, Hall A Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells. Mol Cell Biol. 15:1995;1110-1122.
    • (1995) Mol Cell Biol , vol.15 , pp. 1110-1122
    • Ridley, A.J.1    Comoglio, P.M.2    Hall, A.3
  • 24
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in Rac- And Rho-induced cytoskeletal reorganization
    • Machesky LM, Hall A Role of actin polymerization and adhesion to extracellular matrix in Rac- and Rho-induced cytoskeletal reorganization. J Cell Biol. 138:1997;913-926.
    • (1997) J Cell Biol , vol.138 , pp. 913-926
    • MacHesky, L.M.1    Hall, A.2
  • 26
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma R, Ahmed S, Best A, Lim L The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol Cell Biol. 15:1995;1942-1952.
    • (1995) Mol Cell Biol , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 27
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes CD, Hall A Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:1995;53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 28
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne HR, Sanders DA, McCormick F The GTPase superfamily: conserved structure and molecular mechanism. Nature. 349:1991;117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 31
    • 0025965647 scopus 로고
    • Regulation of binding of RhoB p20 to membranes by its specific regulatory protein, GDP dissociation inhibitor
    • Isomura M, Kikuchi A, Ohga N, Takai Y Regulation of binding of RhoB p20 to membranes by its specific regulatory protein, GDP dissociation inhibitor. Oncogene. 6:1991;119-124.
    • (1991) Oncogene , vol.6 , pp. 119-124
    • Isomura, M.1    Kikuchi, A.2    Ohga, N.3    Takai, Y.4
  • 32
  • 33
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells
    • The emphasis of this review is on molecules that interact with the Rho family GTPases and their roles in the regulation of cytoskeleton and cell adhesion.
    • Kaibuchi K, Kuroda S, Amano M Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu Rev Biochem. 68:1999;459-486. The emphasis of this review is on molecules that interact with the Rho family GTPases and their roles in the regulation of cytoskeleton and cell adhesion.
    • (1999) Annu Rev Biochem , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 34
    • 0032493903 scopus 로고    scopus 로고
    • Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin-mediated cell-cell adhesion
    • This paper reported for the first time the mechanism by which the Rho family GTPases including Cdc42 and Rac1 regulate E-cadherin-mediated cell-cell adhesion. IQGAP1, which is an effector of Cdc42 and Rac1 appears to regulate cell-cell adhesion through the cadherin-catenin pathway acting downstream of Cdc42 and Rac1
    • Kuroda S, Fukata M, Nakagawa M, Fujii K, Nakamura T, Ookubo T, Izawa I, Nagase T, Nomura N, Tani Het al. Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin-mediated cell-cell adhesion. Science. 281:1998;832-835. This paper reported for the first time the mechanism by which the Rho family GTPases including Cdc42 and Rac1 regulate E-cadherin-mediated cell-cell adhesion. IQGAP1, which is an effector of Cdc42 and Rac1 appears to regulate cell-cell adhesion through the cadherin-catenin pathway acting downstream of Cdc42 and Rac1.
    • (1998) Science , vol.281 , pp. 832-835
    • Kuroda, S.1    Fukata, M.2    Nakagawa, M.3    Fujii, K.4    Nakamura, T.5    Ookubo, T.6    Izawa, I.7    Nagase, T.8    Nomura, N.9    Tani, H.10
  • 35
    • 0032948289 scopus 로고    scopus 로고
    • Regulation of cadherin function by Rho and Rac: Modulation by junction maturation and cellular context
    • This paper reported that the regulation of cadherin adhesiveness by the Rho family GTPases is influenced by the maturation status of the junction and the cellular context.
    • Braga VMM, Del Maschio A, Machesky L, Dejana E Regulation of cadherin function by Rho and Rac: modulation by junction maturation and cellular context. Mol Biol Cell. 10:1999;9-22. This paper reported that the regulation of cadherin adhesiveness by the Rho family GTPases is influenced by the maturation status of the junction and the cellular context.
    • (1999) Mol Biol Cell , vol.10 , pp. 9-22
    • Braga, V.M.M.1    Del Maschio, A.2    MacHesky, L.3    Dejana, E.4
  • 36
    • 0033543551 scopus 로고    scopus 로고
    • Cdc42 and Rac1 regulate the interaction of IQGAP1 with β-catenin
    • This paper described that Cdc42 and Rac1 negatively regulate the IQGAP1 function by inhibiting the interaction of IQGAP1 with β-catenin, leading to stabilisation of the cadherin-catenins complex.
    • Fukata M, Kuroda S, Nakagawa M, Kawajiri A, Itoh N, Shoji I, Matsuura Y, Yonehara S, Fujisawa H, Kikuchi A, Kaibuchi K Cdc42 and Rac1 regulate the interaction of IQGAP1 with β-catenin. J Biol Chem. 274:1999;26044-26050. This paper described that Cdc42 and Rac1 negatively regulate the IQGAP1 function by inhibiting the interaction of IQGAP1 with β-catenin, leading to stabilisation of the cadherin-catenins complex.
    • (1999) J Biol Chem , vol.274 , pp. 26044-26050
    • Fukata, M.1    Kuroda, S.2    Nakagawa, M.3    Kawajiri, A.4    Itoh, N.5    Shoji, I.6    Matsuura, Y.7    Yonehara, S.8    Fujisawa, H.9    Kikuchi, A.10    Kaibuchi, K.11
  • 37
    • 0030802038 scopus 로고    scopus 로고
    • Rho proteins: Targets for bacterial toxins
    • Aktories K Rho proteins: targets for bacterial toxins. Trends Microbiol. 5:1997;282-288.
    • (1997) Trends Microbiol , vol.5 , pp. 282-288
    • Aktories, K.1
  • 39
    • 0028087729 scopus 로고
    • The roles of catenins in the cadherin-mediated cell adhesion: Functional analysis of E-cadherin-α-catenin fusion molecules
    • Nagafuchi A, Ishihara S, Tsukita S The roles of catenins in the cadherin-mediated cell adhesion: functional analysis of E-cadherin-α-catenin fusion molecules. J Cell Biol. 127:1994;235-245.
    • (1994) J Cell Biol , vol.127 , pp. 235-245
    • Nagafuchi, A.1    Ishihara, S.2    Tsukita, S.3
  • 40
    • 0029892844 scopus 로고    scopus 로고
    • Mechanism for transition from initial to stable cell-cell adhesion: Kinetic analysis of E-cadherin-mediated adhesion using a quantitative adhesion assay
    • Angres B, Barth A, Nelson WJ Mechanism for transition from initial to stable cell-cell adhesion: kinetic analysis of E-cadherin-mediated adhesion using a quantitative adhesion assay. J Cell Biol. 134:1996;549-557.
    • (1996) J Cell Biol , vol.134 , pp. 549-557
    • Angres, B.1    Barth, A.2    Nelson, W.J.3
  • 41
    • 0033594088 scopus 로고    scopus 로고
    • Functional domains of α-catenin required for the strong state of cadherin-based cell adhesion
    • Imamura Y, Itoh M, Maeno Y, Tsukita S, Nagafuchi A Functional domains of α-catenin required for the strong state of cadherin-based cell adhesion. J Cell Biol. 144:1999;1311-1322.
    • (1999) J Cell Biol , vol.144 , pp. 1311-1322
    • Imamura, Y.1    Itoh, M.2    Maeno, Y.3    Tsukita, S.4    Nagafuchi, A.5
  • 42
    • 0029891491 scopus 로고    scopus 로고
    • IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for Cdc42Hs
    • Hart MJ, Callow MG, Souza B, Polakis P IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for Cdc42Hs. EMBO J. 15:1996;2997-3005.
    • (1996) EMBO J , vol.15 , pp. 2997-3005
    • Hart, M.J.1    Callow, M.G.2    Souza, B.3    Polakis, P.4
  • 45
    • 0031844821 scopus 로고    scopus 로고
    • Activation of Rac and Cdc42 by integrins mediates cell spreading
    • This paper describes that integrin-dependent adhesion of cell to substratum leads to the rapid activation of Cdc42 and Rac.
    • Price LS, Leng J, Schwartz MA, Bokoch GM Activation of Rac and Cdc42 by integrins mediates cell spreading. Mol Biol Cell. 9:1998;1863-1871. This paper describes that integrin-dependent adhesion of cell to substratum leads to the rapid activation of Cdc42 and Rac.
    • (1998) Mol Biol Cell , vol.9 , pp. 1863-1871
    • Price, L.S.1    Leng, J.2    Schwartz, M.A.3    Bokoch, G.M.4
  • 46
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP- binding protein Rho by cell adhesion and the cytoskeleton
    • Plating Swiss 3T3 cells of fibronectin-coated dishes elicits a transient inhibition of Rho, followed by a phase of Rho activation. This indicates that integrin-dependent adhesion of cell to substratum induces Rho activation.
    • Ren XD, Kiosses WB, Schwartz MA Regulation of the small GTP- binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18:1999;578-585. Plating Swiss 3T3 cells of fibronectin-coated dishes elicits a transient inhibition of Rho, followed by a phase of Rho activation. This indicates that integrin-dependent adhesion of cell to substratum induces Rho activation.
    • (1999) EMBO J , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 48
    • 0031009585 scopus 로고    scopus 로고
    • E-cadherin engagement stimulates tyrosine phosphorylation
    • Kinch MS, Petch L, Zhong C, Burridge K E-cadherin engagement stimulates tyrosine phosphorylation. Cell Adhes Commun. 4:1997;425-437.
    • (1997) Cell Adhes Commun , vol.4 , pp. 425-437
    • Kinch, M.S.1    Petch, L.2    Zhong, C.3    Burridge, K.4
  • 49
    • 0030910268 scopus 로고    scopus 로고
    • Interaction of the adaptor protein Shc and the adhesion molecule cadherin
    • Xu Y, Guo DF, Davidson M, Inagami T, Carpenter G Interaction of the adaptor protein Shc and the adhesion molecule cadherin. J Biol Chem. 272:1997;13463-13466.
    • (1997) J Biol Chem , vol.272 , pp. 13463-13466
    • Xu, Y.1    Guo, D.F.2    Davidson, M.3    Inagami, T.4    Carpenter, G.5
  • 50
    • 0032498847 scopus 로고    scopus 로고
    • Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: Corralling and tethering by the membrane skeleton
    • The translational movement of E-cadherin in the plasma membrane in epithelial cells, and the mechanism of its regulation were studied using single particle tracking and optical tweezers
    • Sako Y, Nagafuchi A, Tsukita S, Takeichi M, Kusumi A Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: corralling and tethering by the membrane skeleton. J Cell Biol. 140:1998;1227-1240. The translational movement of E-cadherin in the plasma membrane in epithelial cells, and the mechanism of its regulation were studied using single particle tracking and optical tweezers.
    • (1998) J Cell Biol , vol.140 , pp. 1227-1240
    • Sako, Y.1    Nagafuchi, A.2    Tsukita, S.3    Takeichi, M.4    Kusumi, A.5
  • 51
    • 0026742310 scopus 로고
    • Cadherin-mediated cell-cell adhesion is perturbed by v-Src tyrosine phosphorylation in metastatic fibroblast
    • Matsuyoshi N, Hamaguchi M, Taniguchi S, Nagafuchi A, Tsukita S, Takeichi M Cadherin-mediated cell-cell adhesion is perturbed by v-Src tyrosine phosphorylation in metastatic fibroblast. J Cell Biol. 118:1992;703-714.
    • (1992) J Cell Biol , vol.118 , pp. 703-714
    • Matsuyoshi, N.1    Hamaguchi, M.2    Taniguchi, S.3    Nagafuchi, A.4    Tsukita, S.5    Takeichi, M.6
  • 52
    • 0027507028 scopus 로고
    • Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phophosrylation of the E-cadherin/β-catenin complex in cells transformed with a temperature-sensitive v-SRC gene
    • Behrens J, Vakaet L, Friis R, Winterhager E, Van Roy F, Mareel MM, Birchmeier W Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phophosrylation of the E-cadherin/β-catenin complex in cells transformed with a temperature-sensitive v-SRC gene. J Cell Biol. 120:1993;757-766.
    • (1993) J Cell Biol , vol.120 , pp. 757-766
    • Behrens, J.1    Vakaet, L.2    Friis, R.3    Winterhager, E.4    Van Roy, F.5    Mareel, M.M.6    Birchmeier, W.7
  • 53
    • 84907115825 scopus 로고
    • Tyrosine phosphorylation of β-catenin and plakoglobin enhanced by hepatocyte growth factor and epidermal growth factor in human carcinoma cells
    • Shibamoto S, Hayakawa K, Takeuchi K, Hori T, Oku N, Miyazawa K, Kitamura N, Takeichi M, Ito F Tyrosine phosphorylation of β-catenin and plakoglobin enhanced by hepatocyte growth factor and epidermal growth factor in human carcinoma cells. Cell Adhes Commun. 1:1994;295-305.
    • (1994) Cell Adhes Commun , vol.1 , pp. 295-305
    • Shibamoto, S.1    Hayakawa, K.2    Takeuchi, K.3    Hori, T.4    Oku, N.5    Miyazawa, K.6    Kitamura, N.7    Takeichi, M.8    Ito, F.9
  • 54
    • 0032513297 scopus 로고    scopus 로고
    • Altered cell adhesion activity by pervanadate due to the dissociation of α-catenin from the E-cadherin-catenin complex
    • Pervanadate treatment of cells caused tyrosine phosphorylation of E-cadherin and β-catenin. In the treated cells, a significant amount of α-catenin was dissociated from the E-cadherin-catenins complex.
    • Ozawa M, Kemler R Altered cell adhesion activity by pervanadate due to the dissociation of α-catenin from the E-cadherin-catenin complex. J Biol Chem. 273:1998;6166-6170. Pervanadate treatment of cells caused tyrosine phosphorylation of E-cadherin and β-catenin. In the treated cells, a significant amount of α-catenin was dissociated from the E-cadherin-catenins complex.
    • (1998) J Biol Chem , vol.273 , pp. 6166-6170
    • Ozawa, M.1    Kemler, R.2
  • 55
    • 0029615381 scopus 로고
    • V-Src kinase shifts the cadherin-based cell adhesion from the strong to the weak state and β-catenin is not required for the shift
    • Takeda H, Nagafuchi A, Yonemura S, Tsukita S, Behrens J, Birchmeier W v-Src kinase shifts the cadherin-based cell adhesion from the strong to the weak state and β-catenin is not required for the shift. J Cell Biol. 131:1995;1839-1847.
    • (1995) J Cell Biol , vol.131 , pp. 1839-1847
    • Takeda, H.1    Nagafuchi, A.2    Yonemura, S.3    Tsukita, S.4    Behrens, J.5    Birchmeier, W.6
  • 56
    • 0029160437 scopus 로고
    • Morphogenetic roles of classic cadherins
    • Takeichi M Morphogenetic roles of classic cadherins. Curr Opin Cell Biol. 7:1995;619-627.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 57
    • 0028142230 scopus 로고
    • The motility signal of scatter factor/hepatocyte growth factor mediated through the receptor tyrosine kinase met requires intracellular action of Ras
    • Hartmann G, Weidner KM, Schwarz H, Birchmeier W The motility signal of scatter factor/hepatocyte growth factor mediated through the receptor tyrosine kinase met requires intracellular action of Ras. J Biol Chem. 269:1994;21936-21939.
    • (1994) J Biol Chem , vol.269 , pp. 21936-21939
    • Hartmann, G.1    Weidner, K.M.2    Schwarz, H.3    Birchmeier, W.4
  • 58
    • 0023109112 scopus 로고
    • Nonmitogenic morphoregulatory action of pp60 v-Src on multicellular epithelial structures
    • Warren SL, Nelson WJ Nonmitogenic morphoregulatory action of pp60 v-Src on multicellular epithelial structures. Mol Cell Biol. 7:1987;1326-1337.
    • (1987) Mol Cell Biol , vol.7 , pp. 1326-1337
    • Warren, S.L.1    Nelson, W.J.2
  • 59
    • 0027391509 scopus 로고
    • Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (Rho GDI) in cell motility
    • Takaishi K, Kikuchi A, Kuroda S, Kotani K, Sasaki T, Takai Y Involvement of rho p21 and its inhibitory GDP/GTP exchange protein (Rho GDI) in cell motility. Mol Cell Biol. 13:1993;72-79.
    • (1993) Mol Cell Biol , vol.13 , pp. 72-79
    • Takaishi, K.1    Kikuchi, A.2    Kuroda, S.3    Kotani, K.4    Sasaki, T.5    Takai, Y.6
  • 60
    • 0029131982 scopus 로고
    • Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows
    • Takaishi K, Sasaki T, Kameyama T, Tsukita S, Tsukita S, Takai Y Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene. 11:1995;39-48.
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Takaishi, K.1    Sasaki, T.2    Kameyama, T.3    Tsukita, S.4    Tsukita, S.5    Takai, Y.6
  • 64
    • 0023518424 scopus 로고
    • Expression and distribution of cell adhesion molecule uvomorulin in mouse preimplantation embryos
    • Vestweber D, Gossler A, Boller K, Kemler R Expression and distribution of cell adhesion molecule uvomorulin in mouse preimplantation embryos. Dev Biol. 124:1987;451-456.
    • (1987) Dev Biol , vol.124 , pp. 451-456
    • Vestweber, D.1    Gossler, A.2    Boller, K.3    Kemler, R.4
  • 65
    • 0026735251 scopus 로고
    • Synthesis and phosphorylation of uvomorulin during mouse early development
    • Sefton M, Johnson MH, Clayton L Synthesis and phosphorylation of uvomorulin during mouse early development. Development. 115:1992;313-318.
    • (1992) Development , vol.115 , pp. 313-318
    • Sefton, M.1    Johnson, M.H.2    Clayton, L.3
  • 66
    • 0031573809 scopus 로고    scopus 로고
    • Changes in the pattern of adherens junction-associated β-catenin accompany morphogenesis in the sea urchin embryo
    • Miller JR, McClay DR Changes in the pattern of adherens junction-associated β-catenin accompany morphogenesis in the sea urchin embryo. Dev Biol. 192:1997;310-322.
    • (1997) Dev Biol , vol.192 , pp. 310-322
    • Miller, J.R.1    McClay, D.R.2
  • 67
    • 0031573934 scopus 로고    scopus 로고
    • Characterization of the role of cadherin in regulating cell adhesion during sea urchin development
    • Miller JR, McClay DR Characterization of the role of cadherin in regulating cell adhesion during sea urchin development. Dev Biol. 192:1997;323-339.
    • (1997) Dev Biol , vol.192 , pp. 323-339
    • Miller, J.R.1    McClay, D.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.