메뉴 건너뛰기




Volumn 137, Issue 6, 1997, Pages 1421-1431

The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE;

EID: 0030968177     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.137.6.1421     Document Type: Article
Times cited : (672)

References (75)
  • 2
  • 3
    • 0029782711 scopus 로고    scopus 로고
    • Regulated binding of a PTP1B-like phosphatase to N-cadherin: Control of cadherin mediated adhesion by dephosphorylation of β-catenin
    • Balsamo, J., T Leung, H. Ernst, M.K.B. Zanin, S. Hoffman, and J. Lilien. 1996. Regulated binding of a PTP1B-like phosphatase to N-cadherin: control of cadherin mediated adhesion by dephosphorylation of β-catenin. J. Cell Biol. 134:801-813.
    • (1996) J. Cell Biol. , vol.134 , pp. 801-813
    • Balsamo, J.1    Leung, T.2    Ernst, H.3    Zanin, M.K.B.4    Hoffman, S.5    Lilien, J.6
  • 4
    • 0027507028 scopus 로고
    • Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphoryiation of the E-cadherin/β-catenin complex in cells transformed with a temperature-sensitive v-src gene
    • Behrens, J., L. Vakaet, E. Winterhager, F. Van Roy, M.M. Mareel, and W. Birchmeier. 1993. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphoryiation of the E-cadherin/β-catenin complex in cells transformed with a temperature-sensitive v-src gene. J. Cell Biol. 120:757-766.
    • (1993) J. Cell Biol. , vol.120 , pp. 757-766
    • Behrens, J.1    Vakaet, L.2    Winterhager, E.3    Van Roy, F.4    Mareel, M.M.5    Birchmeier, W.6
  • 6
    • 0025215306 scopus 로고
    • Purified N-cadherin is a potent substrate for the rapid induction of neurite outgrowth
    • Bixby, J.L., and R. Zhang. 1990. Purified N-cadherin is a potent substrate for the rapid induction of neurite outgrowth. J. Cell Biol. 110:1253-1260.
    • (1990) J. Cell Biol. , vol.110 , pp. 1253-1260
    • Bixby, J.L.1    Zhang, R.2
  • 7
    • 0027761007 scopus 로고
    • Expression of Wnt-1 in PC12 cells results in modulation of plakoglobin and E-cadherin and increased cellular adhesion
    • Bradley, R.S., P. Cowin, and A.M.C. Brown. 1993. Expression of Wnt-1 in PC12 cells results in modulation of plakoglobin and E-cadherin and increased cellular adhesion. J. Cell Biol. 123:1857-1865.
    • (1993) J. Cell Biol. , vol.123 , pp. 1857-1865
    • Bradley, R.S.1    Cowin, P.2    Brown, A.M.C.3
  • 8
    • 0029149746 scopus 로고
    • Receptor protein tyrosine phosphatase PTPμ associates with cadherins and catenins in vivo
    • Brady-Kalnay, S., D.L. Rimm, and N.K. Tonks. 1995. Receptor protein tyrosine phosphatase PTPμ associates with cadherins and catenins in vivo. J. Cell Biol. 130:977-986.
    • (1995) J. Cell Biol. , vol.130 , pp. 977-986
    • Brady-Kalnay, S.1    Rimm, D.L.2    Tonks, N.K.3
  • 9
    • 0029085767 scopus 로고
    • Calcium-induced changes in distribution and solubility of cadherins and their associated cytoplasmic proteins in human keratinocytes
    • Braga, V.M.M., K.J. Hodivala, and F.M. Watt. 1995. Calcium-induced changes in distribution and solubility of cadherins and their associated cytoplasmic proteins in human keratinocytes. Cell Adhes. Commun. 3:201-215.
    • (1995) Cell Adhes. Commun. , vol.3 , pp. 201-215
    • Braga, V.M.M.1    Hodivala, K.J.2    Watt, F.M.3
  • 10
    • 0031749258 scopus 로고    scopus 로고
    • Calcium-induced intercellular adhesion of keratinocytes does not involve accumulation of β1 integrins at cell-cell contact sites and does not involve changes in the levels or phosphorylation of catenins
    • In press
    • Braga, V.M.M. N. Hajibagheri, and F.M. Watt. 1997. Calcium-induced intercellular adhesion of keratinocytes does not involve accumulation of β1 integrins at cell-cell contact sites and does not involve changes in the levels or phosphorylation of catenins. Cell Adhesion Com. In press.
    • (1997) Cell Adhesion Com.
    • Braga, V.M.M.1    Hajibagheri, N.2    Watt, F.M.3
  • 11
    • 0029998613 scopus 로고    scopus 로고
    • Lateral dimerization is required for the homophilic binding activity of C-cadherin
    • Brieher, W. M., A.S. Yap, and B.M. Gumbiner. 1996. Lateral dimerization is required for the homophilic binding activity of C-cadherin. J. Cell Biol. 135:487-496.
    • (1996) J. Cell Biol. , vol.135 , pp. 487-496
    • Brieher, W.M.1    Yap, A.S.2    Gumbiner, B.M.3
  • 12
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M., and K. Burridge. 1996. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133:1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 13
    • 0030047838 scopus 로고    scopus 로고
    • Cytoskeleton-membrane interactions
    • Cowin, P.M., and B. Burke. 1996. Cytoskeleton-membrane interactions Curr. Opin. Cell Biol. 8:56-65.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 56-65
    • Cowin, P.M.1    Burke, B.2
  • 15
    • 0027215041 scopus 로고
    • Regulation of human B-cell precursor adhesion to bone marrow stromal cells by cytokines that exert opposing effects on the expression of vascular cell adhesion molecule-1 (VCAM-1)
    • Dittel, B.N., J.B. McCarthy, E.A. Wayner, and T.W. LeBien. 1993. Regulation of human B-cell precursor adhesion to bone marrow stromal cells by cytokines that exert opposing effects on the expression of vascular cell adhesion molecule-1 (VCAM-1). Blood. 81:2272-2282.
    • (1993) Blood , vol.81 , pp. 2272-2282
    • Dittel, B.N.1    McCarthy, J.B.2    Wayner, E.A.3    LeBien, T.W.4
  • 16
    • 0029097186 scopus 로고
    • CDC42 and Rac 1 control different actin-dependent processes in the Drosophila wing disc epithelium
    • Eaton, S., P. Auvinen, L. Luo, Y.N. Jan, and K. Simons. 1995. CDC42 and Rac 1 control different actin-dependent processes in the Drosophila wing disc epithelium. J. Cell Biol. 131:151-164.
    • (1995) J. Cell Biol. , vol.131 , pp. 151-164
    • Eaton, S.1    Auvinen, P.2    Luo, L.3    Jan, Y.N.4    Simons, K.5
  • 17
    • 0030482560 scopus 로고    scopus 로고
    • Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins
    • Fincham, V.J., M. Unlu, V.O. Brunton, J.D. Pitts, J.A. Wyke, and M.C. Frame. 1996. Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins. J. Cell Biol. 135:1551-1564.
    • (1996) J. Cell Biol. , vol.135 , pp. 1551-1564
    • Fincham, V.J.1    Unlu, M.2    Brunton, V.O.3    Pitts, J.D.4    Wyke, J.A.5    Frame, M.C.6
  • 18
    • 0023225091 scopus 로고
    • The relationship between intermediate filaments and microfilaments before and during the formation of desmosomes and adherens-type junctions in mouse epidermal cells
    • Green, K.J., B. Geiger, J.C.R. Jones, J.C. Talian, and R.D. Goldman. 1987.The relationship between intermediate filaments and microfilaments before and during the formation of desmosomes and adherens-type junctions in mouse epidermal cells. J. Cell Biol. 104:1389-1402.
    • (1987) J. Cell Biol. , vol.104 , pp. 1389-1402
    • Green, K.J.1    Geiger, B.2    Jones, J.C.R.3    Talian, J.C.4    Goldman, R.D.5
  • 19
    • 0028982101 scopus 로고
    • Signal transduction by β-catenin
    • Gumbiner, B.M. 1995. Signal transduction by β-catenin. Curr. Biol. 7:634-640.
    • (1995) Curr. Biol. , vol.7 , pp. 634-640
    • Gumbiner, B.M.1
  • 20
    • 0024095524 scopus 로고
    • The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex
    • Gumbiner, B., B. Stevenson, and A. Grimaldi. 1988. The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex. J. Cell Biol. 107:1575-1587.
    • (1988) J. Cell Biol. , vol.107 , pp. 1575-1587
    • Gumbiner, B.1    Stevenson, B.2    Grimaldi, A.3
  • 21
    • 0028947261 scopus 로고
    • A dominant inhibitory version of the small GTP-binding protein Rac disrupts cytoskeletal structures and inhibits developmental cell shape changes in Drosophila
    • Harden, N., H.Y. Loh, W. Chia, and L. Lim. 1995. A dominant inhibitory version of the small GTP-binding protein Rac disrupts cytoskeletal structures and inhibits developmental cell shape changes in Drosophila. Development (Camb.). 121:903-914.
    • (1995) Development (Camb.) , vol.121 , pp. 903-914
    • Harden, N.1    Loh, H.Y.2    Chia, W.3    Lim, L.4
  • 22
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J.H., G.M. Bokoch, C.L. Carpenter, P.A. Jammey, L.A. Taylor, A. Toker, and T.P. Stossel. 1995. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell. 82:643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Jammey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 23
    • 0028258445 scopus 로고
    • Wnt-1 modulates cell - Cell adhesion in mammalian cells by stabilizing β-catenin binding to the cell adhesion protein cadherin
    • Hinck, L., J.W. Nelson, and J. Papkoff. 1994. Wnt-1 modulates cell - cell adhesion in mammalian cells by stabilizing β-catenin binding to the cell adhesion protein cadherin. J. Cell Biol. 124:729-741.
    • (1994) J. Cell Biol. , vol.124 , pp. 729-741
    • Hinck, L.1    Nelson, J.W.2    Papkoff, J.3
  • 24
    • 0024552761 scopus 로고
    • Expression and role of E- and P-cadherin adhesion molecules in embryonic histogenesis. II. Skin morphogenesis
    • Hirai, Y., A. Nose, S. Kobayashi, and M. Takeichi. 1989. Expression and role of E- and P-cadherin adhesion molecules in embryonic histogenesis. II. Skin morphogenesis. Development (Camb.). 105:271-277.
    • (1989) Development (Camb.) , vol.105 , pp. 271-277
    • Hirai, Y.1    Nose, A.2    Kobayashi, S.3    Takeichi, M.4
  • 25
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (Erzin/Radixin/Moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signalling pathways
    • Hirao, M., N. Sato, T. Kondo, S. Yonemura, M. Monden, T. Sasaki, Y. Takai, S. Tsukita, and S. Tsukita. 1996. Regulation mechanism of ERM (Erzin/Radixin/Moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signalling pathways. J. Cell Biol. 135:37-51.
    • (1996) J. Cell Biol. , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, S.8    Tsukita, S.9
  • 27
    • 0027957163 scopus 로고
    • Evidence that cadherins play a role in the downregulation of integrin expression that occurs during keratinocyte terminal differentiation
    • Hodivala, K.J., and F.M. Watt. 1994. Evidence that cadherins play a role in the downregulation of integrin expression that occurs during keratinocyte terminal differentiation. J. Cell Biol. 124:589-600.
    • (1994) J. Cell Biol. , vol.124 , pp. 589-600
    • Hodivala, K.J.1    Watt, F.M.2
  • 28
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases
    • Hotchin, N.A., and A. Hall. 1995. The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases. J. Cell Biol. 131:1857-1865.
    • (1995) J. Cell Biol. , vol.131 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 31
    • 0024464948 scopus 로고
    • Integrin VLA-3: Ultrastructural localization at cell-cell contact sites of human cell cultures
    • Kaufmann, R., D. Frosch, C. Westphal, L. Weber, and C.E. Klein. 1989. Integrin VLA-3: ultrastructural localization at cell-cell contact sites of human cell cultures. J. Cell Biol. 109:1807-1815.
    • (1989) J. Cell Biol. , vol.109 , pp. 1807-1815
    • Kaufmann, R.1    Frosch, D.2    Westphal, C.3    Weber, L.4    Klein, C.E.5
  • 32
    • 0027185632 scopus 로고
    • From cadherins to catenins: Cytoplasmic protein interactions and regulation of cell adhesion
    • Kemler, R. 1993. From cadherins to catenins: cytoplasmic protein interactions and regulation of cell adhesion. Trends Genet. 9:317-321.
    • (1993) Trends Genet. , vol.9 , pp. 317-321
    • Kemler, R.1
  • 34
    • 0029116143 scopus 로고
    • Tyrosine phosphorylation regulates the adhesion of ras-transformed breast epithelia
    • Kinch, M.S., G.J. Clark, C.J. Der, and K. Burridge. 1995. Tyrosine phosphorylation regulates the adhesion of ras-transformed breast epithelia. J. Cell Biol. 130:461-471.
    • (1995) J. Cell Biol. , vol.130 , pp. 461-471
    • Kinch, M.S.1    Clark, G.J.2    Der, C.J.3    Burridge, K.4
  • 35
    • 0028979956 scopus 로고
    • Interaction of α-actinin with the cadherin/catenin cell-cell adhesion complex via α-catenin
    • Knudsen, K., A.P. Soler, K.R. Johnson, and M.J. Wheelock. 1995. Interaction of α-actinin with the cadherin/catenin cell-cell adhesion complex via α-catenin. J. Cell Biol. 130:67-77.
    • (1995) J. Cell Biol. , vol.130 , pp. 67-77
    • Knudsen, K.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 37
    • 0028365071 scopus 로고
    • Cadherin function is required for human keratinocytes to assemble desmosomes and stratify in response to calcium
    • Lewis, J.E., P.J Jensen, and M.J. Wheelock. 1994. Cadherin function is required for human keratinocytes to assemble desmosomes and stratify in response to calcium. J. Invesrig. Dermatol. 102:870-877.
    • (1994) J. Invesrig. Dermatol. , vol.102 , pp. 870-877
    • Lewis, J.E.1    Jensen, P.J.2    Wheelock, M.J.3
  • 38
    • 0028141591 scopus 로고
    • Ankyrin-binding domain of CD44 (GP85) is required for the expression of hvaluronic acid-mediated adhesion function
    • Lokeshwaf, V.B., N. Fregien, and L.Y. Bourguignon. 1994. Ankyrin-binding domain of CD44 (GP85) is required for the expression of hvaluronic acid-mediated adhesion function. J. Cell Biol. 126:1099-1109.
    • (1994) J. Cell Biol. , vol.126 , pp. 1099-1109
    • Lokeshwaf, V.B.1    Fregien, N.2    Bourguignon, L.Y.3
  • 39
    • 0030222377 scopus 로고    scopus 로고
    • Rho: A connection between membrane receptor signalling and the cytoskeleton
    • Machesky, L.M., and A. Hall. 1996. Rho: A connection between membrane receptor signalling and the cytoskeleton. Trends Cell Biol. 6:304-310.
    • (1996) Trends Cell Biol. , vol.6 , pp. 304-310
    • Machesky, L.M.1    Hall, A.2
  • 40
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in Rac- and Rho-induced cytoskeletal reorganization
    • In press
    • Machesky, L.M., and A. Hall. 1997. Role of actin polymerization and adhesion to extracellular matrix in Rac- and Rho-induced cytoskeletal reorganization. J. Cell Biol. In press.
    • (1997) J. Cell Biol.
    • Machesky, L.M.1    Hall, A.2
  • 41
    • 0023552314 scopus 로고
    • Calcium-induced changes in cy1 toskeleton and motility of cultured human keratinocytes
    • Magee, A.I., N.A. Lytton, and F.M. Watt. 1987. Calcium-induced changes in cy1 toskeleton and motility of cultured human keratinocytes. Exp. Cell. Res. 172:43-53.
    • (1987) Exp. Cell. Res. , vol.172 , pp. 43-53
    • Magee, A.I.1    Lytton, N.A.2    Watt, F.M.3
  • 42
    • 0026742310 scopus 로고
    • Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in meiastatic fibroblasts
    • Matsuyoshi, N., M. Hamaguchi, S. Taniguchi, A. Nagafuchi, S. Tsukita, and M. Takeichi. 1992. Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in meiastatic fibroblasts. J. Cell Biol. 118:703-714.
    • (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
  • 43
    • 0025325815 scopus 로고
    • Novel function of the cell adhesion molecule uvomorulin as an inducer of cell surface polarity
    • McNeill, H., M. Ozawa, R. Kemler, and W.J. Nelson. 1990. Novel function of the cell adhesion molecule uvomorulin as an inducer of cell surface polarity. Cell. 62:309-316.
    • (1990) Cell , vol.62 , pp. 309-316
    • McNeill, H.1    Ozawa, M.2    Kemler, R.3    Nelson, W.J.4
  • 44
    • 0343357325 scopus 로고
    • Construction of epithelioid sheets by transfection of mouse sarcoma cells with cDNAs for chicken cell adhesion molecules
    • Mege, R.-M., F. Matsuzaki, W.J. Gallin, J.I. Goldberg, B.A. Cunningham, and G.M. Edelman. 1988. Construction of epithelioid sheets by transfection of mouse sarcoma cells with cDNAs for chicken cell adhesion molecules. Proc. Natl. Acad. Sci. USA. 85:7274-7278.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7274-7278
    • Mege, R.-M.1    Matsuzaki, F.2    Gallin, W.J.3    Goldberg, J.I.4    Cunningham, B.A.5    Edelman, G.M.6
  • 45
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto, S., S. Akiyama, and K.M. Yamada. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science (Wash. DC). 267:883-885.
    • (1995) Science (Wash. DC) , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.2    Yamada, K.M.3
  • 46
    • 0029898417 scopus 로고    scopus 로고
    • Deletion of an amino-terminal sequence stabilizes β-calenin in vivo and promotes hyperphosphorylation of the adenomatous polyposis coli tumor supressor protein
    • Munemitsu, S., I. Albert, B. Rubinfeld, and P. Polakis. 1996. Deletion of an amino-terminal sequence stabilizes β-calenin in vivo and promotes hyperphosphorylation of the adenomatous polyposis coli tumor supressor protein. Mol. Cell. Biol. 16:4088-4094.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4088-4094
    • Munemitsu, S.1    Albert, I.2    Rubinfeld, B.3    Polakis, P.4
  • 47
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C., and A. Hall. 1995. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.1    Hall, A.2
  • 49
    • 0023506138 scopus 로고
    • Antidesmosomal monoclonal antibody in the diagnosis of intracranial tumours
    • Parrish, E.P., P.V. Steart, D.R. Garrod, and R.O. Weller. 1987. Antidesmosomal monoclonal antibody in the diagnosis of intracranial tumours. J. Pathol. 153:265-273.
    • (1987) J. Pathol. , vol.153 , pp. 265-273
    • Parrish, E.P.1    Steart, P.V.2    Garrod, D.R.3    Weller, R.O.4
  • 50
    • 0028266975 scopus 로고
    • A repeating amino acid motif shared by proteins with diverse cellular roles
    • Peifer, M., S. Berg, and A.M. Reynolds. 1994a. A repeating amino acid motif shared by proteins with diverse cellular roles. Cell. 76:789-791.
    • (1994) Cell , vol.76 , pp. 789-791
    • Peifer, M.1    Berg, S.2    Reynolds, A.M.3
  • 51
    • 0028569010 scopus 로고
    • Phosphorylation of the Drosophila adherens junction protein armadillo: Roles for Wingless signal and Zestewhile 3 kinase
    • Peifer, M., L-M. Pai, and M. Casey. 1994b. Phosphorylation of the Drosophila adherens junction protein armadillo: roles for Wingless signal and Zestewhile 3 kinase. Dev. Biol. 166:543-556.
    • (1994) Dev. Biol. , vol.166 , pp. 543-556
    • Peifer, M.1    Pai, L.-M.2    Casey, M.3
  • 52
    • 0001951363 scopus 로고
    • Methods for clonal growth and serial cultivation of normal human epidermal keratinocytes and mesothelial cells
    • R. Baserga, editor. IRL Press, Oxford
    • Rheinwald, J.G. 1989. Methods for clonal growth and serial cultivation of normal human epidermal keratinocytes and mesothelial cells. In Cell Growth and Division. A Practical Approach. R. Baserga, editor. IRL Press, Oxford. 81-94.
    • (1989) Cell Growth and Division. A Practical Approach , pp. 81-94
    • Rheinwald, J.G.1
  • 53
    • 0030267458 scopus 로고    scopus 로고
    • Rho: Theme and variations
    • Ridley, A.J. 1996. Rho: theme and variations. Curr. Biol. 6:1256-1264.
    • (1996) Curr. Biol. , vol.6 , pp. 1256-1264
    • Ridley, A.J.1
  • 54
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and aclin stress fibers in response to growth factors
    • Ridley, A.J., and A. Hall. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and aclin stress fibers in response to growth factors. Cell. 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 55
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., H.F. Paterson, C.L. Johnston, D. Diekman, and A. Hall. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 70:401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekman, D.4    Hall, A.5
  • 56
    • 0028894787 scopus 로고
    • Regulation of scatter factor/ hepatocyte growth factor responses by Ras, Rac and Rho in MDCK cells
    • Ridley, A.J., P.M. Comoglio, and A. Hall. 1995. Regulation of scatter factor/ hepatocyte growth factor responses by Ras, Rac and Rho in MDCK cells. Mol. Cell. Biol. 15:1110-1122.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1110-1122
    • Ridley, A.J.1    Comoglio, P.M.2    Hall, A.3
  • 57
    • 0028981208 scopus 로고
    • Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • Rimm, D.L., E.R. Koslov, P. Kebriaei, C.D. Cianci, and J.S. Morrow. 1995. Alpha 1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proc. Natl. Acad. Sci. USA. 92:8813-8817.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8813-8817
    • Rimm, D.L.1    Koslov, E.R.2    Kebriaei, P.3    Cianci, C.D.4    Morrow, J.S.5
  • 58
    • 0024315423 scopus 로고
    • Morphogenesis of the polarized epithelial cell phenotype
    • Rodriguez-Boulan, I., and W.J. Nelson. 1989. Morphogenesis of the polarized epithelial cell phenotype. Science (Wash. DC). 245:718-725.
    • (1989) Science (Wash. DC) , vol.245 , pp. 718-725
    • Rodriguez-Boulan, I.1    Nelson, W.J.2
  • 60
  • 61
    • 0029097640 scopus 로고
    • Involvement of the GTP binding protein Rho in constitutive endocytosis in Xenupus laevis oocytes
    • Schmalzing, G., H.-P. Richter, A. Hansen, W. Schwartz I. Just, and K. Aktories. 1995. Involvement of the GTP binding protein Rho in constitutive endocytosis in Xenupus laevis oocytes. J. Cell Biol. 130:1319-1332.
    • (1995) J. Cell Biol. , vol.130 , pp. 1319-1332
    • Schmalzing, G.1    Richter, H.-P.2    Hansen, A.3    Schwartz, W.4    Just, I.5    Aktories, K.6
  • 62
    • 84907115825 scopus 로고
    • Tyrosine phosphorvlation of β-catenin and plakoglobin enhanced by hepatocyte growth factor and epidermal growth factor in human carcinoma cells
    • Shibamoto, S., M. Hayakawa, K. Takeuchi, T. Hori, N. Oku, K. Miyazawa, N. Kitamura, M. Takeichi, and F. Ito. 1994. Tyrosine phosphorvlation of β-catenin and plakoglobin enhanced by hepatocyte growth factor and epidermal growth factor in human carcinoma cells. Cell Adhes. Commun. 1:295-305.
    • (1994) Cell Adhes. Commun. , vol.1 , pp. 295-305
    • Shibamoto, S.1    Hayakawa, M.2    Takeuchi, K.3    Hori, T.4    Oku, N.5    Miyazawa, K.6    Kitamura, N.7    Takeichi, M.8    Ito, F.9
  • 63
    • 0024466702 scopus 로고
    • 2+-dependent cell-cell adhesion molecule homologous to mouse placental cadherin: Its low expression in human placental tissues
    • 2+-dependent cell-cell adhesion molecule homologous to mouse placental cadherin: its low expression in human placental tissues. J. Cell Biol. 109:1787-1794.
    • (1989) J. Cell Biol. , vol.109 , pp. 1787-1794
    • Shimoyama, Y.1    Yoshida, T.2    Terada, M.3    Shimosato, Y.4    Abe, O.5    Hirohashi, S.6
  • 64
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the protein fragments of myosin
    • Spudich, J.A., and O.S. Watt. 1971. The regulation of rabbit skeletal muscle contraction I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the protein fragments of myosin. J. Biol. Chem. 246:4866-4872.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4872
    • Spudich, J.A.1    Watt, O.S.2
  • 65
    • 0027756014 scopus 로고
    • Association of the APC tumor suppressor protein with catenins
    • Su, L.-K., B. Vogelstein, and K. W. Kinzier. 1993. Association of the APC tumor suppressor protein with catenins. Science (Wash. DC). 262:1734-1737.
    • (1993) Science (Wash. DC) , vol.262 , pp. 1734-1737
    • Su, L.-K.1    Vogelstein, B.2    Kinzier, K.W.3
  • 66
    • 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., A. Nagafuchi, S. Yonemura, S. Tsukita, J. Behrens, W. Birchmeier, and S. Tsukita. 1995. 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. 131:1839-1847.
    • (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    Tsukita, S.7
  • 67
    • 0025894092 scopus 로고
    • Cadherin cell adhesion receptors as a morphogenetic regulator
    • Takeichi, M. 1991. Cadherin cell adhesion receptors as a morphogenetic regulator. Science (Wash. DC). 251:1451-1455.
    • (1991) Science (Wash. DC) , vol.251 , pp. 1451-1455
    • Takeichi, M.1
  • 68
    • 0027685701 scopus 로고
    • Cadherins in cancer: Implications for invasion and metastasis
    • Takeichi, M. 1993. Cadherins in cancer: implications for invasion and metastasis. Curr. Opin. Cell Biol. 5:806-811.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 806-811
    • Takeichi, M.1
  • 69
    • 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., K. Sugie, M. Hirata, N. Morii, J. Fukata, A. Uchida, H. Imura, and S. Narumiya. 1993. Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho. J. Cell Biol. 120:1529-1537.
    • (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
  • 70
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44and actin-based cytoskeletons
    • Tsukita, S., K. Oishi, N. Sato, J. Sagara, A. Kawai, and S. Tsukita. 1994. ERM family members as molecular linkers between the cell surface glycoprotein CD44and actin-based cytoskeletons. J. Cell Biol. 126:391-401.
    • (1994) J. Cell Biol. , vol.126 , pp. 391-401
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5    Tsukita, S.6
  • 72
    • 0026534152 scopus 로고
    • Regulation of keratinocyte intercellular junction organization and epidermal morphogenesis by E-cadherin
    • Wheelock, M.J., and P.J. Jensen. 1992. Regulation of keratinocyte intercellular junction organization and epidermal morphogenesis by E-cadherin. J. Cell Biol. 117:415-425.
    • (1992) J. Cell Biol. , vol.117 , pp. 415-425
    • Wheelock, M.J.1    Jensen, P.J.2
  • 73
    • 0023377946 scopus 로고
    • Soluble 80-kd fragment of cell-CAM 120/80 disrupts cell-cell adhesion
    • Wheelock, M.J., C.A. Buck, K.B. Bechtol, and C.H. Damsky. 1987. Soluble 80-kd fragment of cell-CAM 120/80 disrupts cell-cell adhesion. J. Cell. Biochem. 34:187-202.
    • (1987) J. Cell. Biochem. , vol.34 , pp. 187-202
    • Wheelock, M.J.1    Buck, C.A.2    Bechtol, K.B.3    Damsky, C.H.4
  • 74
    • 0025918410 scopus 로고
    • An immunofluorescence study of the calcium-induced coordinated reorganization of microfilaments, keratin intermediate filaments, and microtubules in cultured human epidermal keratinocytes
    • Zamansky, G.B., U. Nguyen, and I.-N. Chou. 1991. An immunofluorescence study of the calcium-induced coordinated reorganization of microfilaments, keratin intermediate filaments, and microtubules in cultured human epidermal keratinocytes. J. Investig. Dermatol. 97:985-994.
    • (1991) J. Investig. Dermatol. , vol.97 , pp. 985-994
    • Zamansky, G.B.1    Nguyen, U.2    Chou, I.-N.3
  • 75
    • 0030021649 scopus 로고    scopus 로고
    • Signal transduction and actin filament organization
    • Zigmond, S.H. 1996. Signal transduction and actin filament organization. Curr. Opin. Cell Biol. 8:66-73.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 66-73
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.