메뉴 건너뛰기




Volumn 9, Issue 5, 1997, Pages 683-690

Cadherins, catenins and APC protein: Interplay between cytoskeletal complexes and signaling pathways

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA CATENIN; BETA CATENIN; CADHERIN; CATENIN; PLAKOGLOBIN; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE;

EID: 0342327346     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(97)80122-6     Document Type: Article
Times cited : (491)

References (93)
  • 1
    • 0029899606 scopus 로고    scopus 로고
    • Structural and functional diversity of cadherin superfamily: Are new members of cadherin superfamily involved in signal transduction pathway?
    • Suzuki ST: Structural and functional diversity of cadherin superfamily: are new members of cadherin superfamily involved in signal transduction pathway? J Cell Biochem 1996, 61:531-542.
    • (1996) J Cell Biochem , vol.61 , pp. 531-542
    • Suzuki, S.T.1
  • 2
    • 0030000980 scopus 로고    scopus 로고
    • Cadherin-catenin complex: Protein interactions and their implications for cadherin function
    • Aberle H, Schwartz H, Kemler R: Cadherin-catenin complex: protein interactions and their implications for cadherin function. J Cell Biochem 1996, 61:514-523.
    • (1996) J Cell Biochem , vol.61 , pp. 514-523
    • Aberle, H.1    Schwartz, H.2    Kemler, R.3
  • 3
    • 0029160437 scopus 로고
    • Morphogenetic roles of classic cadherins
    • Takeichi M: Morphogenetic roles of classic cadherins. Curr Opin Cell Biol 1995, 7:619-627.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 4
    • 0030589498 scopus 로고    scopus 로고
    • Cadherins in the developing central nervous system: An adhesive code for segmental and functional subdivisions
    • •]
    • •].
    • (1996) Dev Biol , vol.180 , pp. 413-423
    • Redies, C.1    Takeichi, M.2
  • 5
    • 0030272281 scopus 로고    scopus 로고
    • Cadherins and catenins in development
    • •] are comprehensive reviews on the morphogenetic roles of cadherins in development
    • •] are comprehensive reviews on the morphogenetic roles of cadherins in development.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 685-691
    • Huber, O.1    Bierkamp, C.2    Kemler, R.3
  • 6
    • 0028059290 scopus 로고
    • E-cadherin null mutant embryos fail to form a trophectoderm epithelium
    • Larue L, Ohsugi M, Hirchenhain J, Kemler R: E-cadherin null mutant embryos fail to form a trophectoderm epithelium. Proc Natl Acad Sci USA 1994, 91:8263-8267.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8263-8267
    • Larue, L.1    Ohsugi, M.2    Hirchenhain, J.3    Kemler, R.4
  • 8
    • 0023943310 scopus 로고
    • Guidance of optic nerve fibres by N-cadherin adhesion molecules
    • Matsunaga M, Hatta K, Nagafuchi A, Takeichi M: Guidance of optic nerve fibres by N-cadherin adhesion molecules. Nature 1988, 334:62-64.
    • (1988) Nature , vol.334 , pp. 62-64
    • Matsunaga, M.1    Hatta, K.2    Nagafuchi, A.3    Takeichi, M.4
  • 10
    • 0031042948 scopus 로고    scopus 로고
    • Developmental defects in mouse embryos lacking N-cadherin
    • This paper demonstrates the importance of N-cadherin for different morphogenetic processes during development and is the first paper to show a critical role for N-cadherin in heart development
    • Radice GL, Rayburn H, Matsunami H, Knudsen KA, Takeichi M, Hynes RO: Developmental defects in mouse embryos lacking N-cadherin. Dev Biol 1997, 181:64-78. This paper demonstrates the importance of N-cadherin for different morphogenetic processes during development and is the first paper to show a critical role for N-cadherin in heart development.
    • (1997) Dev Biol , vol.181 , pp. 64-78
    • Radice, G.L.1    Rayburn, H.2    Matsunami, H.3    Knudsen, K.A.4    Takeichi, M.5    Hynes, R.O.6
  • 11
    • 0028972499 scopus 로고
    • Inflammatory bowel disease and adenomas in mice expressing a dominant negative N-cadherin
    • Hermiston ML, Gordon JI: Inflammatory bowel disease and adenomas in mice expressing a dominant negative N-cadherin. Science 1995, 270:1203-1207.
    • (1995) Science , vol.270 , pp. 1203-1207
    • Hermiston, M.L.1    Gordon, J.I.2
  • 12
    • 0029964159 scopus 로고    scopus 로고
    • Forced expression of E-cadherin in the mouse intestinal epithelium slows cell migration and provides evidence for nonautonomous regulation of cell fate in a self-renewing system
    • ••]
    • ••].
    • (1996) Genes Dev , vol.10 , pp. 985-996
    • Hermiston, M.L.1    Wong, M.H.2    Gordon, J.I.3
  • 15
    • 0030014526 scopus 로고    scopus 로고
    • Armadillo is required for adherens junction assembly, cell polarity, and morphogenesis during Drosophila embryogenesis
    • •,16] show that armadillo/β-catenin is required for the integrity of epithelia and normal gastrulation in embryonic development
    • •,16] show that armadillo/β-catenin is required for the integrity of epithelia and normal gastrulation in embryonic development.
    • (1996) J Cell Biol , vol.134 , pp. 133-148
    • Cox, R.T.1    Kirkpatrick, C.2    Peifer, M.3
  • 19
    • 0030464473 scopus 로고    scopus 로고
    • Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion
    • Gives a detailed analysis of E-cadherin and catenin dynamics during early contact formation in epithelial cells
    • Adams CL, Nelson WJ, Smith SJ: Quantitative analysis of cadherin-catenin-actin reorganization during development of cell-cell adhesion. J Cell Biol 1996, 135:1899-1911. Gives a detailed analysis of E-cadherin and catenin dynamics during early contact formation in epithelial cells.
    • (1996) J Cell Biol , vol.135 , pp. 1899-1911
    • Adams, C.L.1    Nelson, W.J.2    Smith, S.J.3
  • 20
    • 0029102071 scopus 로고
    • CAS binds directly to E-cadherin but not to the adenomatous polyposis coli protein or α-catenin
    • CAS binds directly to E-cadherin but not to the adenomatous polyposis coli protein or α-catenin. Mol Cell Biol 1995, 15:4819-4824.
    • (1995) Mol Cell Biol , vol.15 , pp. 4819-4824
    • Daniel, J.M.1    Reynolds, A.B.2
  • 22
    • 0028572556 scopus 로고
    • E-cadherin and APC compete for the interaction with β-catenin and the cytoskeleton
    • Hülsken J, Birchmeier W, Behrens J: E-cadherin and APC compete for the interaction with β-catenin and the cytoskeleton. J Cell Biol 1994, 127:2061-2069.
    • (1994) J Cell Biol , vol.127 , pp. 2061-2069
    • Hülsken, J.1    Birchmeier, W.2    Behrens, J.3
  • 23
    • 0028953279 scopus 로고
    • The APC protein and E-cadherin form similar but independent complexes with α-catenin, β-catenin, and plakoglobin
    • Rubinfeld B, Souza B, Albert I, Munemitsu S, Polakis P: The APC protein and E-cadherin form similar but independent complexes with α-catenin, β-catenin, and plakoglobin. J Biol Chem 1995, 270:5549-5555.
    • (1995) J Biol Chem , vol.270 , pp. 5549-5555
    • Rubinfeld, B.1    Souza, B.2    Albert, I.3    Munemitsu, S.4    Polakis, P.5
  • 24
    • 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, Takeichi M: Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts. J Cell Biol 1992, 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
  • 25
    • 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 MM, 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 1993, 120:757-766.
    • (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
  • 26
    • 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, Nagai Y: p60v-src causes tyrosine phosphorylation and inactivation of the N-cadherin-catenin cell adhesion system. EMBO J 1993, 12:307-314.
    • (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
  • 27
    • 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, Tsukita S: 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 1995, 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
  • 28
    • 0028170977 scopus 로고
    • B-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor
    • Hoschuetzky H, Aberle H, Kemler R: B-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor. J Cell Biol 1994, 127:1375-1380.
    • (1994) J Cell Biol , vol.127 , pp. 1375-1380
    • Hoschuetzky, H.1    Aberle, H.2    Kemler, R.3
  • 29
    • 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 M, 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 Adhesion Commun 1994, 1:295-305.
    • (1994) Cell Adhesion 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
  • 31
    • 0029757471 scopus 로고    scopus 로고
    • Dominant negative inhibition of the association between β-catenin and c-erbB-2 by N-terminally deleted β-catenin suppresses the invasion and metastasis of cancer cells
    • Shibata T, Ochiai A, Kanai Y, Akimoto S, Gotoh M, Yasui N, Machinami R, Hirohashi S: Dominant negative inhibition of the association between β-catenin and c-erbB-2 by N-terminally deleted β-catenin suppresses the invasion and metastasis of cancer cells. Oncogene 1996, 13:883-889.
    • (1996) Oncogene , vol.13 , pp. 883-889
    • Shibata, T.1    Ochiai, A.2    Kanai, Y.3    Akimoto, S.4    Gotoh, M.5    Yasui, N.6    Machinami, R.7    Hirohashi, S.8
  • 32
    • 0029116143 scopus 로고
    • Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia
    • Kinch MS, Clark GJ, Der CJ, Burridge K: Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia. J Cell Biol 1995, 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
  • 33
    • 0029887541 scopus 로고    scopus 로고
    • Intestinal HT-29 cells with dysfunction of E-cadherin show increased pp60src activity and tyrosine phosphorylation of p120-catenin
    • Skoudy A, Llosas MD, Garcia de Herreros A: Intestinal HT-29 cells with dysfunction of E-cadherin show increased pp60src activity and tyrosine phosphorylation of p120-catenin. Biochem J 1996, 317:279-284.
    • (1996) Biochem J , vol.317 , pp. 279-284
    • Skoudy, A.1    Llosas, M.D.2    De Garcia Herreros, A.3
  • 34
    • 0029006254 scopus 로고
    • The interaction of the retina cell surface N-acetyl-galactosaminylphosphotransferase with an endogenous proteoglycan ligand results in inhibition of cadherin-mediated adhesion
    • Balsamo J, Ernst H, Zanin MK, Hoffman S, Lilien J: The interaction of the retina cell surface N-acetyl-galactosaminylphosphotransferase with an endogenous proteoglycan ligand results in inhibition of cadherin-mediated adhesion. J Cell Biol 1995, 129:1391 -1401.
    • (1995) J Cell Biol , vol.129 , pp. 1391-1401
    • Balsamo, J.1    Ernst, H.2    Zanin, M.K.3    Hoffman, S.4    Lilien, J.5
  • 35
    • 0029149746 scopus 로고
    • Receptor protein tyrosine phosphatase PTPμ, associates with cadherins and catenins in vivo
    • Brady-Kalnay SM, Rimm DL, Tonks NK: Receptor protein tyrosine phosphatase PTPμ, associates with cadherins and catenins in vivo. J Cell Biol 1995, 130:977-986.
    • (1995) J Cell Biol , vol.130 , pp. 977-986
    • Brady-Kalnay, S.M.1    Rimm, D.L.2    Tonks, N.K.3
  • 38
    • 0029782711 scopus 로고    scopus 로고
    • Regulated binding of PTP1B-like phosphatase to N-cadherin: Control of cadherin-mediated adhesion by dephosphorylation of β-catenin
    • •], together with [35,39], show binding of protein tyrosine phosphatases to the cadherin-catenin complex
    • •], together with [35,39], show binding of protein tyrosine phosphatases to the cadherin-catenin complex.
    • (1996) J Cell Biol , vol.134 , pp. 801-813
    • Balsamo, J.1    Leung, T.2    Ernst, H.3    Zanin, M.K.4    Hoffman, S.5    Lilien, J.6
  • 39
    • 0030904004 scopus 로고    scopus 로고
    • A novel protein-tyrosine phosphatase related to the homotypically adhering K and u, receptors
    • Cheng J, Wu K, Armanini M, O'Rourke N, Dowbenko D, Lasky LA: A novel protein-tyrosine phosphatase related to the homotypically adhering K and u, receptors. J Biol Chem 1997, 272:7264-7277.
    • (1997) J Biol Chem , vol.272 , pp. 7264-7277
    • Cheng, J.1    Wu, K.2    Armanini, M.3    O'Rourke, N.4    Dowbenko, D.5    Lasky, L.A.6
  • 40
    • 0029125639 scopus 로고
    • Protein tyrosine phosphatases as adhesion receptors
    • Brady-Kalnay SM, Tonks NK: Protein tyrosine phosphatases as adhesion receptors. Curr Opin Cell Biol 1995, 7:650-657.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 650-657
    • Brady-Kalnay, S.M.1    Tonks, N.K.2
  • 42
    • 0029003699 scopus 로고
    • Cell adhesion and signal transduction: The armadillo connection
    • Peifer M: Cell adhesion and signal transduction: the armadillo connection. Trends Cell Biol 1995, 5:224-229.
    • (1995) Trends Cell Biol , vol.5 , pp. 224-229
    • Peifer, M.1
  • 43
    • 0029964851 scopus 로고    scopus 로고
    • Signal transduction through β-catenin and specification of cell fate during embryogenesis
    • Miller JR, Moon RT: Signal transduction through β-catenin and specification of cell fate during embryogenesis. Genes Dev 1996, 10:2527-2539.
    • (1996) Genes Dev , vol.10 , pp. 2527-2539
    • Miller, J.R.1    Moon, R.T.2
  • 44
    • 0028971587 scopus 로고
    • The C. elegans gene lin-44, which controls the polarity of certain asymmetric cell divisions, encodes a Wnt protein and acts cell nonautonomously
    • Herman MA, Vassilieva LL, Horvitz HR, Shaw JE, Herman RK: The C. elegans gene lin-44, which controls the polarity of certain asymmetric cell divisions, encodes a Wnt protein and acts cell nonautonomously. Cell 1995, 83:101 -110.
    • (1995) Cell , vol.83 , pp. 101-110
    • Herman, M.A.1    Vassilieva, L.L.2    Horvitz, H.R.3    Shaw, J.E.4    Herman, R.K.5
  • 45
    • 0029994517 scopus 로고    scopus 로고
    • A new member of the frizzled family from Drosophila functions as a Wingless receptor
    • This paper describes the identification of members of the frizzled family as the Wnt/Wingless receptors. See also [46]
    • Bhanot P, Brink M, Samos CH, Hsieh JC, Wang Y, Macke JP, Andrew D, Nathans J, Nusse R: A new member of the frizzled family from Drosophila functions as a Wingless receptor. Nature 1996, 382:225-230. This paper describes the identification of members of the frizzled family as the Wnt/Wingless receptors. See also [46].
    • (1996) Nature , vol.382 , pp. 225-230
    • Bhanot, P.1    Brink, M.2    Samos, C.H.3    Hsieh, J.C.4    Wang, Y.5    Macke, J.P.6    Andrew, D.7    Nathans, J.8    Nusse, R.9
  • 46
  • 48
    • 0029683606 scopus 로고    scopus 로고
    • The axis-inducing activity, stability, and subcellular distribution of β-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3
    • Describes the effects of glycogen synthase kinase-3β on the phosphorylation, stability and localization of β-catenin in Xenopus embryos
    • Yost C, Torres M, Miller JR, Huang E, Kimelman D, Moon RT: The axis-inducing activity, stability, and subcellular distribution of β-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3. Genes Dev 1996, 10:1443-1454. Describes the effects of glycogen synthase kinase-3β on the phosphorylation, stability and localization of β-catenin in Xenopus embryos.
    • (1996) Genes Dev , vol.10 , pp. 1443-1454
    • Yost, C.1    Torres, M.2    Miller, J.R.3    Huang, E.4    Kimelman, D.5    Moon, R.T.6
  • 49
    • 0030199669 scopus 로고    scopus 로고
    • B-catenin translocation into nuclei demarcates the dorsalizing centers in frog and fish embryos
    • Schneider S, Steinbeisser H, Warga RM, Hausen P: B-catenin translocation into nuclei demarcates the dorsalizing centers in frog and fish embryos. Mech Dev 1996, 57:191-198.
    • (1996) Mech Dev , vol.57 , pp. 191-198
    • Schneider, S.1    Steinbeisser, H.2    Warga, R.M.3    Hausen, P.4
  • 51
    • 0030917251 scopus 로고    scopus 로고
    • A versatile transcriptional effector of wingless signaling
    • Nusse R: A versatile transcriptional effector of wingless signaling. Cell 1997, 89:321-323.
    • (1997) Cell , vol.89 , pp. 321-323
    • Nusse, R.1
  • 53
    • 0028987249 scopus 로고
    • Regulation of intracellular β-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein
    • Munemitsu S, Albert I, Souza B, Rubinfeld B, Polakis P: Regulation of intracellular β-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein. Proc Natl Acad Sci USA 1995, 92:3046-3050.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3046-3050
    • Munemitsu, S.1    Albert, I.2    Souza, B.3    Rubinfeld, B.4    Polakis, P.5
  • 56
    • 0028047389 scopus 로고
    • wingless signal and Zeste-white 3 kinase trigger opposing changes in the intracelllar distribution of Armadillo
    • Peifer M, Sweeton D, Casey M, Weischaus E: wingless signal and Zeste-white 3 kinase trigger opposing changes in the intracelllar distribution of Armadillo. Development 1994, 120:369-380.
    • (1994) Development , vol.120 , pp. 369-380
    • Peifer, M.1    Sweeton, D.2    Casey, M.3    Weischaus, E.4
  • 60
    • 0345343608 scopus 로고    scopus 로고
    • Nuclear localization of β-catenin by interaction with transcription factor LEF-1
    • •• provides evidence that the E-cadherin gene is a downstream target of the β-catenin-LEF-1 complex
    • ••) provides evidence that the E-cadherin gene is a downstream target of the β-catenin-LEF-1 complex.
    • (1996) Mech Dev , vol.59 , pp. 3-10
    • Huber, O.1    Korn, R.2    McLaughlin, J.3    Ohsugi, M.4    Herrmann, B.G.5    Kemler, R.6
  • 62
    • 0028783457 scopus 로고
    • pop-1 encodes an HMG box protein required for the specification of a mesoderm precursor in early C elegans embryos
    • Lin R, Thompson S, Priess JR: pop-1 encodes an HMG box protein required for the specification of a mesoderm precursor in early C elegans embryos. Cell 1995, 83:599-609.
    • (1995) Cell , vol.83 , pp. 599-609
    • Lin, R.1    Thompson, S.2    Priess, J.R.3
  • 64
    • 0030979996 scopus 로고    scopus 로고
    • LEF-1, a nuclear factor coordinating signaling inputs from wingless and decapentaplegic
    • The paper shows transcriptional activation of the ultrabithorax enhancer by the β-catenin-lymphoid enhancer-binding factor-1 complex. This provides the first evidence for a downstream gene target of the complex of β-catenin and transcription factor in the Wnt/Wingless pathway in Drosophila
    • Riese J, Yu X, Munnerlyn A, Eresh S, Hsu SC, Grosschedl R, Bienz M: LEF-1, a nuclear factor coordinating signaling inputs from wingless and decapentaplegic. Cell 1997, 88:777-787. The paper shows transcriptional activation of the ultrabithorax enhancer by the β-catenin-lymphoid enhancer-binding factor-1 complex. This provides the first evidence for a downstream gene target of the complex of β-catenin and transcription factor in the Wnt/Wingless pathway in Drosophila.
    • (1997) Cell , vol.88 , pp. 777-787
    • Riese, J.1    Yu, X.2    Munnerlyn, A.3    Eresh, S.4    Hsu, S.C.5    Grosschedl, R.6    Bienz, M.7
  • 65
    • 0023919954 scopus 로고
    • Two-tiered regulation of spatially patterned engrailed gene expression during Drosophila embryogenesis
    • DiNardo S, Sher E, Heemskerk-Jongens J, Kassis JA, O'Farrell PH: Two-tiered regulation of spatially patterned engrailed gene expression during Drosophila embryogenesis. Nature 1988, 332:604-609.
    • (1988) Nature , vol.332 , pp. 604-609
    • DiNardo, S.1    Sher, E.2    Heemskerk-Jongens, J.3    Kassis, J.A.4    O'Farrell, P.H.5
  • 66
    • 0027192975 scopus 로고
    • Indirect autoregulation of a homeotic Drosophila gene mediated by extracellular signaling
    • Thuringer F, Bienz M: Indirect autoregulation of a homeotic Drosophila gene mediated by extracellular signaling. Proc Natl Acad Sci USA 1993, 90:3899-3903.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3899-3903
    • Thuringer, F.1    Bienz, M.2
  • 67
    • 0030601956 scopus 로고    scopus 로고
    • Activation of Siamois by the Wnt pathway
    • Brannon M, Kimelman D: Activation of Siamois by the Wnt pathway. Dev Biol 1996, 180:344-347.
    • (1996) Dev Biol , vol.180 , pp. 344-347
    • Brannon, M.1    Kimelman, D.2
  • 68
    • 0031040143 scopus 로고    scopus 로고
    • Induction of the primary dorsalizing center in Xenopus by the Wnt/GSK/β-catenin signaling pathway, but not by Vg1, Activin or Noggin
    • •], which supports a role for β-catenin in the Wnt signaling pathway in inducing the primary dorsalizing center
    • •], which supports a role for β-catenin in the Wnt signaling pathway in inducing the primary dorsalizing center.
    • (1997) Development , vol.124 , pp. 453-460
    • Fagotto, F.1    Guger, K.2    Gumbine, B.M.3
  • 69
  • 70
    • 0029846334 scopus 로고    scopus 로고
    • Maternal β-catenin establishes a 'dorsal signal' in early Xenopus embryos
    • This paper provides evidence that β-catenin can induce the formation of dorsal axial structures in a non-cell-autonomous way
    • Wylie C, Kofron M, Payne C, Anderson R, Hosobuchi M, Joseph E, Heasman J: Maternal β-catenin establishes a 'dorsal signal' in early Xenopus embryos. Development 1996, 122:2987-2996. This paper provides evidence that β-catenin can induce the formation of dorsal axial structures in a non-cell-autonomous way.
    • (1996) Development , vol.122 , pp. 2987-2996
    • Wylie, C.1    Kofron, M.2    Payne, C.3    Anderson, R.4    Hosobuchi, M.5    Joseph, E.6    Heasman, J.7
  • 72
    • 0029768676 scopus 로고    scopus 로고
    • An in vivo structure-function study of armadillo, the β-catenin homologue, reveals both separate and overlapping regions of the protein required for cell adhesion and for wingless signaling
    • •]
    • •].
    • (1996) J Cell Biol , vol.134 , pp. 1283-1300
    • Orsulic, S.1    Peifer, M.2
  • 74
    • 0029995674 scopus 로고    scopus 로고
    • Uncoupling cadherin-based adhesion from wingless signalling in Drosophila
    • •] analyze the relationship between cell-cell adhesion and Wnt/Wingless signaling
    • •] analyze the relationship between cell-cell adhesion and Wnt/Wingless signaling.
    • (1996) Nature , vol.383 , pp. 627-630
    • Sanson, B.1    White, P.2    Vincent, J.P.3
  • 75
    • 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 WJ, 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 1994, 124:729-741.
    • (1994) J Cell Biol , vol.124 , pp. 729-741
    • Hinck, L.1    Nelson, W.J.2    Papkoff, J.3
  • 76
    • 0027761007 scopus 로고
    • Expression of Wnt-1 in PC12 cells results in modulation of plakoglobin and E-cadherin and increased cellular adhesion
    • Bradley RS, Cowin P, Brown AM: Expression of Wnt-1 in PC12 cells results in modulation of plakoglobin and E-cadherin and increased cellular adhesion. J Cell Biol 1993, 123:1857-1865.
    • (1993) J Cell Biol , vol.123 , pp. 1857-1865
    • Bradley, R.S.1    Cowin, P.2    Brown, A.M.3
  • 77
    • 0029312503 scopus 로고
    • Oncogene activation and oncogene cooperation in MMTV-induced mouse mammary cancer
    • Van Leeuwen F, Nusse R: Oncogene activation and oncogene cooperation in MMTV-induced mouse mammary cancer. Semin Cancer Biol 1995, 6:127-133.
    • (1995) Semin Cancer Biol , vol.6 , pp. 127-133
    • Van Leeuwen, F.1    Nusse, R.2
  • 78
    • 0028957642 scopus 로고
    • Mutations in the APC gene and their implications for protein structure and function
    • Polakis P: Mutations in the APC gene and their implications for protein structure and function. Curr Opin Genet Dev 1995, 5:66-71.
    • (1995) Curr Opin Genet Dev , vol.5 , pp. 66-71
    • Polakis, P.1
  • 79
    • 0030592517 scopus 로고    scopus 로고
    • Lessons from hereditary colorectal cancer
    • Kinzler KW, Vogelstein B: Lessons from hereditary colorectal cancer. Cell 1996, 87:159-170.
    • (1996) Cell , vol.87 , pp. 159-170
    • Kinzler, K.W.1    Vogelstein, B.2
  • 80
    • 0029669950 scopus 로고    scopus 로고
    • A mutated β-catenin gene encodes a melanoma-specific antigen recognized by tumor infiltrating lymphocytes
    • Robbins PF, El-Gamil M, Li YF, Kawakami Y, Loftus D, Appella E, Rosenberg SA: A mutated β-catenin gene encodes a melanoma-specific antigen recognized by tumor infiltrating lymphocytes. J Exp Med 1996, 183:1185-1192.
    • (1996) J Exp Med , vol.183 , pp. 1185-1192
    • Robbins, P.F.1    El-Gamil, M.2    Li, Y.F.3    Kawakami, Y.4    Loftus, D.5    Appella, E.6    Rosenberg, S.A.7
  • 83
    • 0030900696 scopus 로고    scopus 로고
    • Stabilization of β-catenin by genetic defects in melanoma cell lines
    • •• provide evidence that loss of adenomatous poly posis coli protein function or β-catenin mutation results in the accumulation of active β-catenin-transcription factor complexes and cancer formation
    • ••) provide evidence that loss of adenomatous poly posis coli protein function or β-catenin mutation results in the accumulation of active β-catenin-transcription factor complexes and cancer formation.
    • (1997) Science , vol.275 , pp. 1790-1792
    • Rubinfeld, B.1    Robbins, P.2    El-Gamil, M.3    Albert, I.4    Porfiri, E.5    Polakis, P.6
  • 85
    • 0029846832 scopus 로고    scopus 로고
    • Two independent domains of hDlg are sufficient for subcellular targeting: The PDZ1-2 conformational unit and an alternatively spliced domain
    • Lue RA, Brandin E, Chan EP, Branton D: Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain. J Cell Biol 1996, 135:1125-1137.
    • (1996) J Cell Biol , vol.135 , pp. 1125-1137
    • Lue, R.A.1    Brandin, E.2    Chan, E.P.3    Branton, D.4
  • 86
    • 0002626928 scopus 로고    scopus 로고
    • Role for the tumor suppressor adenomatous polyposis coli protein in epithelial migration and adhesion: A hypothesis
    • Edited by Cowin P, Klymkowsky MW. New York: Chapman and Hall
    • Näthke IS, Barth AIM, Nelson WJ: Role for the tumor suppressor adenomatous polyposis coli protein in epithelial migration and adhesion: a hypothesis. In Cytoskeletal-Membrane Interactions and Signal Transduction, edn 1. Edited by Cowin P, Klymkowsky MW. New York: Chapman and Hall; 1997:103-110.
    • (1997) Cytoskeletal-Membrane Interactions and Signal Transduction, Edn 1 , pp. 103-110
    • Näthke, I.S.1    Barth, A.I.M.2    Nelson, W.J.3
  • 88
    • 0027930066 scopus 로고
    • The APC gene product associates with microtubules in vivo and promotes their assembly in vitro
    • Munemitsu S, Souza B, Muller O, Albert I, Rubinfeld B, Polakis P: The APC gene product associates with microtubules in vivo and promotes their assembly in vitro. Cancer Res 1994, 54:3676-3681.
    • (1994) Cancer Res , vol.54 , pp. 3676-3681
    • Munemitsu, S.1    Souza, B.2    Muller, O.3    Albert, I.4    Rubinfeld, B.5    Polakis, P.6
  • 89
    • 0029982877 scopus 로고    scopus 로고
    • The adenomatous polyposis coli tumor suppressor protein localizes to plasma membrane sites involved in active cell migration
    • This paper shows microtubule-dependent clustering of adenomatous polyposis coli (APC) protein in membrane extensions and, together with [88], suggests a function of APC protein in organizing microtubules
    • Näthke IS, Adams CL, Polakis P, Sellin JH, Nelson WJ: The adenomatous polyposis coli tumor suppressor protein localizes to plasma membrane sites involved in active cell migration. J Cell Biol 1996, 134:165-179. This paper shows microtubule-dependent clustering of adenomatous polyposis coli (APC) protein in membrane extensions and, together with [88], suggests a function of APC protein in organizing microtubules.
    • (1996) J Cell Biol , vol.134 , pp. 165-179
    • Näthke, I.S.1    Adams, C.L.2    Polakis, P.3    Sellin, J.H.4    Nelson, W.J.5
  • 92
    • 0030923749 scopus 로고    scopus 로고
    • Dynamics of β-catenin interactions with APC protein regulate epithelial tubulogenesis
    • in press. This paper describes that overexpression of amino-terminal-deleted β-catenin inhibits epithelial morphogenesis
    • Pollack AL, Barth AIM, Altschuler Y, Nelson WJ, Mostov KE: Dynamics of β-catenin interactions with APC protein regulate epithelial tubulogenesis. J Cell Biol 1997, in press. This paper describes that overexpression of amino-terminal-deleted β-catenin inhibits epithelial morphogenesis.
    • (1997) J Cell Biol
    • Pollack, A.L.1    Barth, A.I.M.2    Altschuler, Y.3    Nelson, W.J.4    Mostov, K.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.