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Volumn 9, Issue 11, 1998, Pages 905-918

Identification of a novel mechanism of regulation of the adherens junction by E1A, Rac1, and cortical actin filaments that contributes to tumor progression

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA CATENIN; PROTEIN KINASE; RAS PROTEIN; VIRUS PROTEIN;

EID: 0031734679     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (21)

References (98)
  • 1
    • 0000014184 scopus 로고
    • Decreased mutual adhesiveness, a property of cells from squamous cell carcinomas
    • Coman, D. R. Decreased mutual adhesiveness, a property of cells from squamous cell carcinomas. Cancer Res., 1: 625-629, 1944.
    • (1944) Cancer Res. , vol.1 , pp. 625-629
    • Coman, D.R.1
  • 2
    • 0026723902 scopus 로고
    • Epithelial morphogenesis
    • Gumbiner, B. M. Epithelial morphogenesis. Cell, 69: 385-387, 1992.
    • (1992) Cell , vol.69 , pp. 385-387
    • Gumbiner, B.M.1
  • 3
    • 0029066824 scopus 로고
    • Adherens junction proteins in tumor progression
    • Birchmeier, W., Hulsken, J., and Behrens, J. Adherens junction proteins in tumor progression. Cancer Surv., 24: 129-140, 1995.
    • (1995) Cancer Surv. , vol.24 , pp. 129-140
    • Birchmeier, W.1    Hulsken, J.2    Behrens, J.3
  • 4
    • 0026518504 scopus 로고
    • Molecular organization of the uvomorulin-catenin complex
    • Ozawa, M., and Kemler, R. Molecular organization of the uvomorulin-catenin complex. J. Cell Biol., 116: 989-996, 1992.
    • (1992) J. Cell Biol. , vol.116 , pp. 989-996
    • Ozawa, M.1    Kemler, R.2
  • 5
    • 0026316099 scopus 로고
    • A homolog of the armadillo protein in Drosophila (plakoglobin) associated with E-cadherin
    • Washington DC
    • McCrea, P. D., Turck, C. W., and Gumbiner, B. A homolog of the armadillo protein in Drosophila (plakoglobin) associated with E-cadherin. Science (Washington DC), 254: 1359-1361, 1991.
    • (1991) Science , vol.254 , pp. 1359-1361
    • McCrea, P.D.1    Turck, C.W.2    Gumbiner, B.3
  • 6
    • 1842390685 scopus 로고
    • Cell binding function of E-cadherin is regulated by the cytoplasmic domain
    • Nagafuchi, A., and Takeichi, M. Cell binding function of E-cadherin is regulated by the cytoplasmic domain. EMBO J., 7: 3679-3684, 1988.
    • (1988) EMBO J. , vol.7 , pp. 3679-3684
    • Nagafuchi, A.1    Takeichi, M.2
  • 7
    • 0027685701 scopus 로고
    • Cadherins in cancer: Implications for invasion and metastasis
    • Takeichi, M. Cadherins in cancer: implications for invasion and metastasis. Curr. Opin. Cell Biol., 5: 806-811, 1993.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 806-811
    • Takeichi, M.1
  • 12
    • 0028060061 scopus 로고
    • Reduced E-cadherin expression correlates with increased invasiveness in colorectal carcinoma cell lines
    • Kinsella, A. R., Lepts, G. C., Hill, C. L., and Jones, M. Reduced E-cadherin expression correlates with increased invasiveness in colorectal carcinoma cell lines. Clin. Exp. Metastasis, 12: 335-342, 1994.
    • (1994) Clin. Exp. Metastasis , vol.12 , pp. 335-342
    • Kinsella, A.R.1    Lepts, G.C.2    Hill, C.L.3    Jones, M.4
  • 14
    • 0026630994 scopus 로고
    • Identification of neural α-catenin as a key regulator of cadherin function and multicellular organization
    • Hirano, S., Kimoto, N., Shimoyama, Y., Hirihashi, S., and Takeichi, M. Identification of neural α-catenin as a key regulator of cadherin function and multicellular organization. Cell, 70: 293-301, 1992.
    • (1992) Cell , vol.70 , pp. 293-301
    • Hirano, S.1    Kimoto, N.2    Shimoyama, Y.3    Hirihashi, S.4    Takeichi, M.5
  • 15
    • 0027185168 scopus 로고
    • Reduction of E-cadherin levels and deletion of the α-catenin gene in human prostate cancer cells
    • Morton, R. A., Ewing, C. M., Nagafuchi, A., Tsukita, S., and Isaacs, W. B. Reduction of E-cadherin levels and deletion of the α-catenin gene in human prostate cancer cells. Cancer Res., 53: 3585-3590, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 3585-3590
    • Morton, R.A.1    Ewing, C.M.2    Nagafuchi, A.3    Tsukita, S.4    Isaacs, W.B.5
  • 16
    • 0028179098 scopus 로고
    • Inverse relation of E-cadherin and autocrine motility factor receptor expression as a prognostic factor in patients with bladder carcinomas
    • Otto, T., Birchmeier, W., Schmidt, U., Hinke, A., Schipper, J., Rubben, H., and Raz, A. Inverse relation of E-cadherin and autocrine motility factor receptor expression as a prognostic factor in patients with bladder carcinomas. Cancer Res., 54: 3120-3123, 1994.
    • (1994) Cancer Res. , vol.54 , pp. 3120-3123
    • Otto, T.1    Birchmeier, W.2    Schmidt, U.3    Hinke, A.4    Schipper, J.5    Rubben, H.6    Raz, A.7
  • 17
    • 0028603343 scopus 로고
    • TGF-β induced transdifferentiation of mammary epithelial cells to mesenchymal cells: Involvement of type I receptors
    • Miettinen, P. J., Ebner, R., Lopez, A. R., and Derynck, R. TGF-β induced transdifferentiation of mammary epithelial cells to mesenchymal cells: involvement of type I receptors. J. Cell Biol., 127: 2021-2036, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 2021-2036
    • Miettinen, P.J.1    Ebner, R.2    Lopez, A.R.3    Derynck, R.4
  • 18
    • 0028305906 scopus 로고
    • Overexpression of ErbB2 in human mammary epithelial cells signals inhibition of transcription of the E-cadherin gene
    • D'Souza, B., and Taylor-Papadimitriou, J. Overexpression of ErbB2 in human mammary epithelial cells signals inhibition of transcription of the E-cadherin gene. Proc. Natl. Acad. Sci. USA, 91: 7202-7206, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7202-7206
    • D'Souza, B.1    Taylor-Papadimitriou, J.2
  • 19
    • 0028170977 scopus 로고
    • β-Catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor
    • Hoschuetzky, H., Aberle, H., and Kemler, R. β-Catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor. J. Cell Biol., 127: 1375-1381, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 1375-1381
    • Hoschuetzky, H.1    Aberle, H.2    Kemler, R.3
  • 20
    • 84907115825 scopus 로고
    • Tyrosine phosphorylation of β-catenin and plakoglobin enhanced by hepatocyte growth factor and epidermal growth factor in human carcinoma cells. Cell Adhes
    • Shibamoto, S., Hayakawa, M., Takeuchi, K., Hori, T., Oku, N., Miyazawa, K., Kitamura, N., Takeichi, M., and 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: 295-305, 1994.
    • (1994) 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
  • 21
    • 0027507028 scopus 로고
    • Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation 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, M. M., and Birchmeier, W. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/ β-catenin complex in cells transformed with a temperature-sensitive v-SRC gene. J. Cell Biol., 120: 757-766, 1993.
    • (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
  • 22
    • 0027459346 scopus 로고
    • P60v-src causes tyrosine phosphorylation and inactivation of the N-cadherin-catenin cell adhesion system
    • Hamaguchi, M., Matsuyoshi, N., Ohnishi, Y., Gotoh, B., Takeichi, M., and Nagai, Y. p60v-src causes tyrosine phosphorylation and inactivation of the N-cadherin-catenin cell adhesion system. EMBO J., 12: 307-314, 1993.
    • (1993) EMBO J. , vol.12 , pp. 307-314
    • Hamaguchi, M.1    Matsuyoshi, N.2    Ohnishi, Y.3    Gotoh, B.4    Takeichi, M.5    Nagai, Y.6
  • 23
    • 0026742310 scopus 로고
    • Cadherin mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts
    • Matsuyoshi, N., Hamaguchi, M., Taniguchi, S., Nagafuchi, A., Tsukita, S., and Takeichi, M. Cadherin mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts. J. Cell Biol., 118: 703-714, 1992.
    • (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
  • 24
    • 0029116143 scopus 로고
    • Tyrosine phosphorylation regulates the adhesions of Ras-transformed breast epithelia
    • Kinch, M. S., Clark, G. J., Der, C. J., and Burridge, K. Tyrosine phosphorylation regulates the adhesions of Ras-transformed breast epithelia. J. Cell Biol., 130: 461-471, 1995.
    • (1995) J. Cell Biol. , vol.130 , pp. 461-471
    • Kinch, M.S.1    Clark, G.J.2    Der, C.J.3    Burridge, K.4
  • 25
    • 0029102071 scopus 로고
    • cas binds directly to E-cadherin but not to the APC protein or α-catenin
    • cas binds directly to E-cadherin but not to the APC protein or α-catenin. Mol. Cell. Biol., 15: 4819-4824, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4819-4824
    • Daniel, J.M.1    Reynold, A.B.2
  • 27
    • 0028593497 scopus 로고
    • E-Cadherin mediates adherens junction organization through protein kinase C
    • Lewis, J. E., Jensen, P. J., Johnson, K. R., and Wheelock, M. J. E-Cadherin mediates adherens junction organization through protein kinase C. J. Cell Sci., 108: 3615-3621, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 3615-3621
    • Lewis, J.E.1    Jensen, P.J.2    Johnson, K.R.3    Wheelock, M.J.4
  • 28
    • 0027289308 scopus 로고
    • Regulation of E-cadherin-mediated adhesion by muscarinic acetylcholine receptors in small cell lung carcinoma
    • Williams, C. L., Hayes, V. Y., Hummel, A. M., Tarara, J. E., and Halsey, T. J. Regulation of E-cadherin-mediated adhesion by muscarinic acetylcholine receptors in small cell lung carcinoma. J. Cell Biol., 121: 643-654, 1993.
    • (1993) J. Cell Biol. , vol.121 , pp. 643-654
    • Williams, C.L.1    Hayes, V.Y.2    Hummel, A.M.3    Tarara, J.E.4    Halsey, T.J.5
  • 29
    • 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., Cowin, P., and Brown, A. M. C. 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.
    • (1993) J. Cell Biol. , vol.123 , pp. 1857-1865
    • Bradley, R.S.1    Cowin, P.2    Brown, A.M.C.3
  • 30
    • 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., Nelson, W. J., and Papkoff, J. 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.
    • (1994) J. Cell Biol. , vol.124 , pp. 729-741
    • Hinck, L.1    Nelson, W.J.2    Papkoff, J.3
  • 31
    • 0020571212 scopus 로고
    • Identification and purification of a cell surface glycoprotein mediating intercellular adhesion in embryonic and adult tissue
    • Damsky, C. H., Richa, J., Solter, D., Knudsen, K., and Buck, C. A. Identification and purification of a cell surface glycoprotein mediating intercellular adhesion in embryonic and adult tissue. Cell, 34: 455-466, 1983.
    • (1983) Cell , vol.34 , pp. 455-466
    • Damsky, C.H.1    Richa, J.2    Solter, D.3    Knudsen, K.4    Buck, C.A.5
  • 34
    • 0030047838 scopus 로고    scopus 로고
    • Cytoskeleton-membrane interactions
    • Cowin, P., and Burke, B. Cytoskeleton-membrane interactions. Curr. Opin. Cell Biol., 8: 56-65, 1996.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 56-65
    • Cowin, P.1    Burke, B.2
  • 35
    • 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., and 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: 235-245, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 235-245
    • Nagafuchi, A.1    Ishihara, S.2    Tsukita, S.3
  • 36
    • 0028981208 scopus 로고
    • α1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • Rimm, D. L., Koslov, E. R., Kebriaei, P., Cianci, C. D., and Morrow, J. S. α1(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.
    • (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
  • 37
    • 0028979956 scopus 로고
    • Interaction of α-actinin with the cadherin/catenin cell adhesion complex via α-catenin
    • Knudsen, K. A., Soler, A. P., Johnson, K. R., and Wheelock, M. J. Interaction of α-actinin with the cadherin/catenin cell adhesion complex via α-catenin. J. Cell Biol., 130: 67-79, 1995.
    • (1995) J. Cell Biol. , vol.130 , pp. 67-79
    • Knudsen, K.A.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 38
    • 0027722747 scopus 로고
    • Epithelial cell adhesion and development of cell surface polarity: Possible mechanisms for modulation of cadherin function, organization and distribution
    • Nathke, I. S., Hinck, L. E., and Nelson, W. J. Epithelial cell adhesion and development of cell surface polarity: possible mechanisms for modulation of cadherin function, organization and distribution. J. Cell Sci., 17 (Suppl.): 139-145, 1993.
    • (1993) J. Cell Sci. , vol.17 , Issue.SUPPL. , pp. 139-145
    • Nathke, I.S.1    Hinck, L.E.2    Nelson, W.J.3
  • 39
    • 0027723788 scopus 로고
    • Catenins as mediators of the cytoplasmic functions of cadherins
    • Gumbiner, B. M., and McCrea, P. D. Catenins as mediators of the cytoplasmic functions of cadherins. J. Cell Sci., 17 (Suppl.): 155-158, 1993.
    • (1993) J. Cell Sci. , vol.17 , Issue.SUPPL. , pp. 155-158
    • Gumbiner, B.M.1    McCrea, P.D.2
  • 40
    • 0029097186 scopus 로고
    • CDC42 and rac1 control different actin-dependent processes in the Drosophila wing disc epithelium
    • Eaton, S., Auvinen, P., Luo, L., Jan, Y. N., and Simons, K. CDC42 and rac1 control different actin-dependent processes in the Drosophila wing disc epithelium. J. Cell Biol., 131: 151-164, 1995.
    • (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
  • 41
    • 0025331713 scopus 로고
    • Defective gap-junctional communication associated with imaginal disc overgrowth and degeneration caused by mutations in the dco gene in Drosophila
    • Jursnich, V. A., Fraser, S. E., Held, L. I., Ryerse, J., and Bryant, P. Defective gap-junctional communication associated with imaginal disc overgrowth and degeneration caused by mutations in the dco gene in Drosophila. Dev. Biol., 140: 413-429, 1990.
    • (1990) Dev. Biol. , vol.140 , pp. 413-429
    • Jursnich, V.A.1    Fraser, S.E.2    Held, L.I.3    Ryerse, J.4    Bryant, P.5
  • 42
    • 0025941465 scopus 로고
    • The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions
    • Woods, D., and Bryant, P. The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell, 66: 451-464, 1991.
    • (1991) Cell , vol.66 , pp. 451-464
    • Woods, D.1    Bryant, P.2
  • 43
    • 0028051486 scopus 로고
    • The Drosophila lethal(2) giant larvae tumor suppressor protein is a component of the cytoskeleton
    • Strand, D., Raska, I., and Mechler, B. The Drosophila lethal(2) giant larvae tumor suppressor protein is a component of the cytoskeleton. J. Cell Biol., 127: 1345-1360, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 1345-1360
    • Strand, D.1    Raska, I.2    Mechler, B.3
  • 44
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon, N., and Hall, A. Rho, Rac, and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol., 9: 86-92, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 45
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga, V. M., Machesky, L. M., Hall, A., and Hotchin, N. A. The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J. Cell Biol., 137: 1421-1431, 1997.
    • (1997) J. Cell Biol. , vol.137 , pp. 1421-1431
    • Braga, V.M.1    Machesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 46
    • 0018970029 scopus 로고
    • Partial transformation of primary rat cells by the leftmost 4.5% fragment of adenovirus 5 DNA
    • Houweling, A., van der Elsen, P. J., and Van der Eb, A. J. Partial transformation of primary rat cells by the leftmost 4.5% fragment of adenovirus 5 DNA. Virology, 105: 537-550, 1980.
    • (1980) Virology , vol.105 , pp. 537-550
    • Houweling, A.1    Van Der Elsen, P.J.2    Van Der Eb, A.J.3
  • 47
    • 0032581941 scopus 로고    scopus 로고
    • The C-terminus of E1A regulates tumor progression and epithelial cell differentiation
    • Fischer, R. S., and Quinlan, M. P. The C-terminus of E1A regulates tumor progression and epithelial cell differentiation. Virology, 249: 427-439, 1998.
    • (1998) Virology , vol.249 , pp. 427-439
    • Fischer, R.S.1    Quinlan, M.P.2
  • 48
    • 0023227354 scopus 로고
    • Growth factor(s) produced during infection with an adenovirus variant stimulates proliferation of nonestablished epithelial cells
    • Quinlan, M. P., Sullivan, N., and Grodzicker, T. Growth factor(s) produced during infection with an adenovirus variant stimulates proliferation of nonestablished epithelial cells. Proc. Natl. Acad. Sci. USA, 84: 3283-3287, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3283-3287
    • Quinlan, M.P.1    Sullivan, N.2    Grodzicker, T.3
  • 49
    • 0023743073 scopus 로고
    • Growth factor induction by the adenovirus type 5 E1A 12S protein is required for immortalization of primary epithelial cells
    • Quinlan, M. P., Whyte, P., and Grodzicker, T. Growth factor induction by the adenovirus type 5 E1A 12S protein is required for immortalization of primary epithelial cells. Mol. Cell. Biol., 8: 3191-3203, 1988.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3191-3203
    • Quinlan, M.P.1    Whyte, P.2    Grodzicker, T.3
  • 50
    • 0030458205 scopus 로고    scopus 로고
    • Induction of a complex between rasGAP and a novel 110 kD protein is required for immortalization of primary epithelial cells by the E1a 12S oncoprotein of adenovirus
    • Gopalakrishnan, S., Fischer, R. S., and Quinlan, M. P. Induction of a complex between rasGAP and a novel 110 kD protein is required for immortalization of primary epithelial cells by the E1A 12S oncoprotein of adenovirus. Oncogene, 13: 2659-2669, 1996.
    • (1996) Oncogene , vol.13 , pp. 2659-2669
    • Gopalakrishnan, S.1    Fischer, R.S.2    Quinlan, M.P.3
  • 51
    • 0030955636 scopus 로고    scopus 로고
    • Immortalization of primary epithelial cells by E1A 12S requires late, second exon-encoded functions in addition to complex formation with pRb and p300
    • Gopalakrishnan, S., Douglas, J. L., and Quinlan, M. P. Immortalization of primary epithelial cells by E1A 12S requires late, second exon-encoded functions in addition to complex formation with pRb and p300. Cell Growth Differ., 8: 541-551, 1997.
    • (1997) Cell Growth Differ. , vol.8 , pp. 541-551
    • Gopalakrishnan, S.1    Douglas, J.L.2    Quinlan, M.P.3
  • 52
    • 0026557712 scopus 로고
    • Immortalization of primary epithelial cells requires first and second exon functions of Ad5 12S
    • Quinlan, M. P., and Douglas, J. L. Immortalization of primary epithelial cells requires first and second exon functions of Ad5 12S. J. Virol., 66: 2020-2030, 1992.
    • (1992) J. Virol. , vol.66 , pp. 2020-2030
    • Quinlan, M.P.1    Douglas, J.L.2
  • 53
    • 0023374802 scopus 로고
    • Mutational analysis of the adenovirus E1a gene: The role of transcriptional regulation in transformation
    • Schneider, J. F., Fisher, F., Goding, C. R., and Jones, N. C. Mutational analysis of the adenovirus E1a gene: the role of transcriptional regulation in transformation. EMBO J., 6: 2053-2060, 1987.
    • (1987) EMBO J. , vol.6 , pp. 2053-2060
    • Schneider, J.F.1    Fisher, F.2    Goding, C.R.3    Jones, N.C.4
  • 54
    • 0028113326 scopus 로고
    • E1A induces the expression of epithelial characteristics
    • Frisch, S. M. E1A induces the expression of epithelial characteristics. J. Cell Biol., 127: 1085-1096, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 1085-1096
    • Frisch, S.M.1
  • 55
    • 0029099116 scopus 로고
    • Modulation of E-cadherin localization in cells expressing wild-type E1A 12S or hypertransforming mutants
    • Gopalakrishnan, S., and Quinlan, M. P. Modulation of E-cadherin localization in cells expressing wild-type E1A 12S or hypertransforming mutants. Cell Growth Differ., 6: 985-998, 1995.
    • (1995) Cell Growth Differ. , vol.6 , pp. 985-998
    • Gopalakrishnan, S.1    Quinlan, M.P.2
  • 56
    • 0020520517 scopus 로고
    • Adenovirus early region 1A enables viral and cellular transforming genes to transform primary cells in culture
    • Ruley, H. E. Adenovirus early region 1A enables viral and cellular transforming genes to transform primary cells in culture. Nature (Lond.), 304: 602-606, 1983.
    • (1983) Nature (Lond.) , vol.304 , pp. 602-606
    • Ruley, H.E.1
  • 57
    • 0024574323 scopus 로고
    • Enhanced ras oncogene-mediated cell transformation and tumorigenesis by adenovirus 2 mutants lacking the c-terminal region of E1a protein
    • Subramanian, T., La Regina, M., and Chinnadurai, G. Enhanced ras oncogene-mediated cell transformation and tumorigenesis by adenovirus 2 mutants lacking the c-terminal region of E1a protein. Oncogene, 4: 415-420, 1989.
    • (1989) Oncogene , vol.4 , pp. 415-420
    • Subramanian, T.1    La Regina, M.2    Chinnadurai, G.3
  • 58
    • 0027509346 scopus 로고
    • A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras-mediated transformation, tumorigenesis and metastasis
    • Boyd, J. M., Subramanian, T., Schaeper, U., La Regina, M., Bayley, S., and Chinnadurai, G. A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras-mediated transformation, tumorigenesis and metastasis. EMBO J., 12: 469-478, 1993.
    • (1993) EMBO J. , vol.12 , pp. 469-478
    • Boyd, J.M.1    Subramanian, T.2    Schaeper, U.3    La Regina, M.4    Bayley, S.5    Chinnadurai, G.6
  • 59
    • 0023665003 scopus 로고
    • Functional domains of adenovirus type 5 E1a proteins
    • Lillie, J. W., Loewenstein, P. M., Green, M. R., and Green, M. Functional domains of adenovirus type 5 E1a proteins. Cell, 50: 1091-1100, 1987.
    • (1987) Cell , vol.50 , pp. 1091-1100
    • Lillie, J.W.1    Loewenstein, P.M.2    Green, M.R.3    Green, M.4
  • 60
    • 0023864316 scopus 로고
    • An N-terminal region of adenovirus E1A essential for cell transformation and induction of an epithelial cell growth factor
    • Subramanian, T., Kuppuswamy, M., Nasr, R. J., and Chinnadurai, G. An N-terminal region of adenovirus E1A essential for cell transformation and induction of an epithelial cell growth factor. Oncogene, 2: 105-112, 1988.
    • (1988) Oncogene , vol.2 , pp. 105-112
    • Subramanian, T.1    Kuppuswamy, M.2    Nasr, R.J.3    Chinnadurai, G.4
  • 61
    • 0023925848 scopus 로고
    • Two regions of the adenovirus early region 1A proteins are required for transformation
    • Whyte, P., Ruley, H. E., and Harlow, E. Two regions of the adenovirus early region 1A proteins are required for transformation. J. Virol., 62: 257-265, 1988.
    • (1988) J. Virol. , vol.62 , pp. 257-265
    • Whyte, P.1    Ruley, H.E.2    Harlow, E.3
  • 62
    • 0025936354 scopus 로고
    • Modulation of transformation of primary epithelial cells by the second exon of the Ad5 E1A 12S gene
    • Douglas, J. L., Gopalakrishnan, S., and Quinlan, M. P. Modulation of transformation of primary epithelial cells by the second exon of the Ad5 E1A 12S gene. Oncogene, 6: 2093-2103, 1991.
    • (1991) Oncogene , vol.6 , pp. 2093-2103
    • Douglas, J.L.1    Gopalakrishnan, S.2    Quinlan, M.P.3
  • 63
    • 0031928106 scopus 로고    scopus 로고
    • Rac1 and extracellularly regulated kinase activation are sufficient for E1A-dependent cooperative transformation of primary epithelial cells, but progression can only be modulated by E1A or Rac1
    • Fischer, R. S., Zheng, Y., and Quinlan, M. P. Rac1 and extracellularly regulated kinase activation are sufficient for E1A-dependent cooperative transformation of primary epithelial cells, but progression can only be modulated by E1A or Rac1. Cell Growth Differ., 9: 209-221, 1998.
    • (1998) Cell Growth Differ. , vol.9 , pp. 209-221
    • Fischer, R.S.1    Zheng, Y.2    Quinlan, M.P.3
  • 64
    • 0026577380 scopus 로고
    • Enhanced invasive properties of rat embryo fibroblasts transformed by adenovirus E1A mutants with deletions in the carboxyl-terminal exon
    • Linder, S., Popowicz, P., Svensson, C., Marshall, H., Bondesson, M., and Akusjarvi, G. Enhanced invasive properties of rat embryo fibroblasts transformed by adenovirus E1A mutants with deletions in the carboxyl-terminal exon. Oncogene, 7: 439-443, 1992.
    • (1992) Oncogene , vol.7 , pp. 439-443
    • Linder, S.1    Popowicz, P.2    Svensson, C.3    Marshall, H.4    Bondesson, M.5    Akusjarvi, G.6
  • 65
    • 0025858522 scopus 로고
    • Requirement of the C-terminal region of adenovirus E1a for cell transformation in cooperation with E1b
    • Subramanian, T., Malstrom, S. E., and Chinnadurai, G. Requirement of the C-terminal region of adenovirus E1a for cell transformation in cooperation with E1b. Oncogene, 6: 1171-1173, 1991.
    • (1991) Oncogene , vol.6 , pp. 1171-1173
    • Subramanian, T.1    Malstrom, S.E.2    Chinnadurai, G.3
  • 66
    • 0023121272 scopus 로고
    • Adenovirus E1A 12S protein induces DNA synthesis and proliferation in primary epithelial cells in both the presence and absence of serum
    • Quinlan, M. P., and Grodzicker, T. Adenovirus E1A 12S protein induces DNA synthesis and proliferation in primary epithelial cells in both the presence and absence of serum. J. Virol., 61: 673-682, 1987.
    • (1987) J. Virol. , vol.61 , pp. 673-682
    • Quinlan, M.P.1    Grodzicker, T.2
  • 67
    • 0031949105 scopus 로고    scopus 로고
    • Expression of the Rb binding regions of E1A enables efficient transformation of primary epithelial cells by v-src
    • Fischer, R. S., and Quinlan, M. P. Expression of the Rb binding regions of E1A enables efficient transformation of primary epithelial cells by v-src. J. Virol., 72: 2815-2824, 1998.
    • (1998) J. Virol. , vol.72 , pp. 2815-2824
    • Fischer, R.S.1    Quinlan, M.P.2
  • 68
    • 0029664368 scopus 로고    scopus 로고
    • Binding of GSK3β to the APC-β-catenin complex and regulation of complex assembly
    • Washington DC
    • Rubinfeld, B., Albert, I., Porfiri, E., Fiol, C., Munernitsu, S., and Polakis, P. Binding of GSK3β to the APC-β-catenin complex and regulation of complex assembly. Science (Washington DC), 272: 1023-1026, 1996.
    • (1996) Science , vol.272 , pp. 1023-1026
    • Rubinfeld, B.1    Albert, I.2    Porfiri, E.3    Fiol, C.4    Munernitsu, S.5    Polakis, P.6
  • 70
    • 0029040123 scopus 로고
    • Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex
    • Jou, T. S., Stewart, D. B., Stappert, J., Nelson, W. J., and Mars, J. A. Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex. Proc. Natl. Acad. Sci. USA, 92: 5067-5071, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5067-5071
    • Jou, T.S.1    Stewart, D.B.2    Stappert, J.3    Nelson, W.J.4    Mars, J.A.5
  • 71
    • 0030464473 scopus 로고    scopus 로고
    • Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion
    • Adams, C. L., Nelson, W. J., and Smith, S. J. Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion. J. Cell Biol., 135: 1899-1911, 1996.
    • (1996) J. Cell Biol. , vol.135 , pp. 1899-1911
    • Adams, C.L.1    Nelson, W.J.2    Smith, S.J.3
  • 72
    • 0028305138 scopus 로고
    • Dynamics of cadherin/catenin complex formation: Novel protein interactions and pathways of complex assembly
    • Hinck, L., Nathke, I. S., Papkoff, J., and Nelson, W. J. Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly. J. Cell Biol., 125: 1327-1340, 1994.
    • (1994) J. Cell Biol. , vol.125 , pp. 1327-1340
    • Hinck, L.1    Nathke, I.S.2    Papkoff, J.3    Nelson, W.J.4
  • 73
    • 0028289669 scopus 로고
    • Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells
    • Nathke, I. S., Hinck, L., Swedlow, J. R., Papkoff, J., and Nelson, W. J. Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells. J. Cell Biol., 125: 1341-1352, 1994.
    • (1994) J. Cell Biol. , vol.125 , pp. 1341-1352
    • Nathke, I.S.1    Hinck, L.2    Swedlow, J.R.3    Papkoff, J.4    Nelson, W.J.5
  • 74
  • 79
    • 0028168318 scopus 로고
    • Expression of E-cadherin and a-catenin molecules in human breast cancer tissues and association with clinicopathological features
    • Takayama, T., Shiozaki, H., Inoue, M., Tamura, S., Oka, H., and Kadowaki, T. Expression of E-cadherin and a-catenin molecules in human breast cancer tissues and association with clinicopathological features. Int. J. Oncol., 5: 775-780, 1994.
    • (1994) Int. J. Oncol. , vol.5 , pp. 775-780
    • Takayama, T.1    Shiozaki, H.2    Inoue, M.3    Tamura, S.4    Oka, H.5    Kadowaki, T.6
  • 80
    • 0030743389 scopus 로고    scopus 로고
    • Expression of wild-type α-catenin protein in cells with a mutant α-catenin gene restores both growth regulation and tumor suppression function
    • Bullions, L. C., Notterman, D. A., Chung, L. S., and Levine, A. J. Expression of wild-type α-catenin protein in cells with a mutant α-catenin gene restores both growth regulation and tumor suppression function. Mol. Cell. Biol., 17: 4501-4508, 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4501-4508
    • Bullions, L.C.1    Notterman, D.A.2    Chung, L.S.3    Levine, A.J.4
  • 81
    • 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., and Nelson, W. J. 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: 549-557, 1996.
    • (1996) J. Cell Biol. , vol.134 , pp. 549-557
    • Angres, B.1    Barth, A.2    Nelson, W.J.3
  • 82
    • 0023577552 scopus 로고
    • Calcium-dependent cell-cell adhesion molecules (cadherins): Subclass specificities and possible involvement of actin bundles
    • Hirano, S., Nose, A., Hatta, K., Kawakami, A., and Takeichi, M. Calcium-dependent cell-cell adhesion molecules (cadherins): subclass specificities and possible involvement of actin bundles. J. Cell. Biol., 105: 2501-2510, 1987.
    • (1987) J. Cell. Biol. , vol.105 , pp. 2501-2510
    • Hirano, S.1    Nose, A.2    Hatta, K.3    Kawakami, A.4    Takeichi, M.5
  • 83
    • 0024451982 scopus 로고
    • The cytoplasmic domain of cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species
    • Ozawa, M., Baribult, H., and Kemler, R. The cytoplasmic domain of cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species. EMBO J., 8: 1711-1717, 1989.
    • (1989) EMBO J. , vol.8 , pp. 1711-1717
    • Ozawa, M.1    Baribult, H.2    Kemler, R.3
  • 84
    • 0028800305 scopus 로고
    • Activation of rac1, rhoA, and mitogen-activated protein kinases is required for ras transformation
    • Khosravi-Far, R., Solski, P. A., Clark, G. J., Kinch, M. S., and Der, C. J. Activation of rac1, rhoA, and mitogen-activated protein kinases is required for ras transformation. Mol. Cell. Biol., 15: 6443-6453, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6443-6453
    • Khosravi-Far, R.1    Solski, P.A.2    Clark, G.J.3    Kinch, M.S.4    Der, C.J.5
  • 85
    • 0029055812 scopus 로고
    • The small GTP-binding proteins rac1 and cdc42 regulate the activity of the JNK/SAPK signalling pathway
    • Coso, O. A., Chiariello, M., Yu, J. C., Teramoto, H., Crespo, P., Xu, N., Miki, T., and Gutkind, J. S. The small GTP-binding proteins rac1 and cdc42 regulate the activity of the JNK/SAPK signalling pathway. Cell, 81: 1137-1146, 1995.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 86
    • 0029070887 scopus 로고
    • Selective activation of the JNK signalling cascade and c-jun transcriptional activity by the small GTPases rac and cdc42Hs
    • Minden, A., Lin, A., Claret, F-X., Abo, A., and Karin, M. Selective activation of the JNK signalling cascade and c-jun transcriptional activity by the small GTPases rac and cdc42Hs. Cell, 81: 1147-1157, 1995.
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.-X.3    Abo, A.4    Karin, M.5
  • 88
    • 0031026132 scopus 로고    scopus 로고
    • Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways
    • Westwick, J. K., Lambert, Q. T., Clark, G. J., Symons, M., Van, A. L., Pestell, R. G., and Der, C. J. Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways. Mol. Cell. Biol., 17: 1324-1335, 1997.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1324-1335
    • Westwick, J.K.1    Lambert, Q.T.2    Clark, G.J.3    Symons, M.4    Van, A.L.5    Pestell, R.G.6    Der, C.J.7
  • 89
    • 0030610386 scopus 로고    scopus 로고
    • Cell-junctional and cytoskeletal organization in mouse blastocysts lacking E-cadherin
    • Ohsugi, M., Larue, L., Schwarz, H., and Kemler, R. Cell-junctional and cytoskeletal organization in mouse blastocysts lacking E-cadherin. Dev. Biol., 185: 261-271, 1997.
    • (1997) Dev. Biol. , vol.185 , pp. 261-271
    • Ohsugi, M.1    Larue, L.2    Schwarz, H.3    Kemler, R.4
  • 90
    • 0028821093 scopus 로고
    • Cell-to-cell adherens junction formation and actin filament organization: Similarities and differences between non-polarized fibroblasts and polarized epithelial cells
    • Yonemura, S., Itoh, M., Nagafuchi, A., and Tsukita, S. Cell-to-cell adherens junction formation and actin filament organization: similarities and differences between non-polarized fibroblasts and polarized epithelial cells. J. Cell Sci., 108: 127-142, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 127-142
    • Yonemura, S.1    Itoh, M.2    Nagafuchi, A.3    Tsukita, S.4
  • 92
    • 0027489248 scopus 로고
    • Disorganization of microfilaments and intermediate filaments interferes with the assembly and stability of desmosomes in MDCK epithelial cells
    • Pasdar, M., and Li, Z. Disorganization of microfilaments and intermediate filaments interferes with the assembly and stability of desmosomes in MDCK epithelial cells. Cell Motil. Cytoskelet., 26: 163-180, 1993.
    • (1993) Cell Motil. Cytoskelet. , vol.26 , pp. 163-180
    • Pasdar, M.1    Li, Z.2
  • 93
    • 0029985110 scopus 로고    scopus 로고
    • Tumour suppressive properties of the adenovirus 5 E1A oncogene
    • Mymryk, J. S. Tumour suppressive properties of the adenovirus 5 E1A oncogene. Oncogene, 13: 1581-1589, 1996.
    • (1996) Oncogene , vol.13 , pp. 1581-1589
    • Mymryk, J.S.1
  • 94
    • 0023934299 scopus 로고
    • Cell type-dependent transformation by adenovirus 5 E1A proteins
    • Kuppuswamy, M., and Chinnadurai, G. Cell type-dependent transformation by adenovirus 5 E1A proteins. Oncogene, 2: 567-572, 1988.
    • (1988) Oncogene , vol.2 , pp. 567-572
    • Kuppuswamy, M.1    Chinnadurai, G.2
  • 95
    • 0020404981 scopus 로고
    • Activation of the T24 bladder carcinoma transforming gene is linked to a single amino acid change
    • Taparowsky, E., Suard, Y., Fasano, O., Shimuzu, K., Goldfarb, M., and Wigler, M. Activation of the T24 bladder carcinoma transforming gene is linked to a single amino acid change. Nature (Lond.), 300: 762-765, 1982.
    • (1982) Nature (Lond.) , vol.300 , pp. 762-765
    • Taparowsky, E.1    Suard, Y.2    Fasano, O.3    Shimuzu, K.4    Goldfarb, M.5    Wigler, M.6
  • 97
    • 0001116582 scopus 로고
    • Immunofluorescence microscopy of the cytoskeleton: Double and triple immunofluorescence
    • J. E. Celis (ed.), San Diego, CA: Academic Press
    • Herzog, M., Dreager, A., Ehler, E., and Small, J. V. Immunofluorescence microscopy of the cytoskeleton: double and triple immunofluorescence. In: J. E. Celis (ed.), Cell Biology: A Laboratory Handbook, Vol. 2, pp. 355-374. San Diego, CA: Academic Press, 1994.
    • (1994) Cell Biology: A Laboratory Handbook , vol.2 , pp. 355-374
    • Herzog, M.1    Dreager, A.2    Ehler, E.3    Small, J.V.4
  • 98
    • 0029910050 scopus 로고    scopus 로고
    • Radicicol inhibits tyrosine phosphorylation of mitotic Src substrate Sam68 and retards subsequent exit from mitosis of Src-transformed cells
    • Pillay, I., Nakano, H., and Sharma, S. V. Radicicol inhibits tyrosine phosphorylation of mitotic Src substrate Sam68 and retards subsequent exit from mitosis of Src-transformed cells. Cell Growth Differ., 7: 1487-1499, 1996.
    • (1996) Cell Growth Differ. , vol.7 , pp. 1487-1499
    • Pillay, I.1    Nakano, H.2    Sharma, S.V.3


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