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Volumn 8, Issue 1, 1998, Pages 95-102

β-catenin: A key mediator of Wnt signaling

Author keywords

[No Author keywords available]

Indexed keywords

BETA CATENIN; LYMPHOID ENHANCER FACTOR 1; PROTEIN; TRANSCRIPTION FACTOR;

EID: 0031888098     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(98)80068-3     Document Type: Article
Times cited : (684)

References (51)
  • 1
    • 0030000980 scopus 로고    scopus 로고
    • Cadherin - Catenin complex: Protein interactions and their implications for cadherin function
    • Aberle H, Schwartz H, Kemler H. Cadherin - catenin complex: protein interactions and their implications for cadherin function. J Cell Biochem. 61:1996;514-523.
    • (1996) J Cell Biochem , vol.61 , pp. 514-523
    • Aberle, H.1    Schwartz, H.2    Kemler, H.3
  • 2
    • 0026316099 scopus 로고
    • A homolog of the Drosophila protein armadillo (Plakoglobin) associates with E-cadherin
    • McCrea PD, Turck CW, Gumbiner B. A homolog of the Drosophila protein armadillo (Plakoglobin) associates with E-cadherin. Science. 254:1991;1359-1361.
    • (1991) Science , vol.254 , pp. 1359-1361
    • McCrea, P.D.1    Turck, C.W.2    Gumbiner, B.3
  • 3
    • 0028447438 scopus 로고
    • Drosophila wingless: A paradigm for the function and mechanism of Wnt signaling
    • Siegfried P, Perrimon N. Drosophila wingless: a paradigm for the function and mechanism of Wnt signaling. Bioessays. 16:1994;395-404.
    • (1994) Bioessays , vol.16 , pp. 395-404
    • Siegfried, P.1    Perrimon, N.2
  • 4
    • 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. 10:1996;2527-2539.
    • (1996) Genes Dev , vol.10 , pp. 2527-2539
    • Miller, J.R.1    Moon, R.T.2
  • 5
    • 0342711244 scopus 로고    scopus 로고
    • Gut reaction to Wnt signaling in worms
    • Han M. Gut reaction to Wnt signaling in worms. Cell. 90:1997;581-584.
    • (1997) Cell , vol.90 , pp. 581-584
    • Han, M.1
  • 6
    • 0026772731 scopus 로고
    • Wnt genes
    • Nusse R, Varmus HE. Wnt genes. Cell. 69:1992;1073-1087.
    • (1992) Cell , vol.69 , pp. 1073-1087
    • Nusse, R.1    Varmus, H.E.2
  • 7
    • 0029994517 scopus 로고    scopus 로고
    • A new member of the frizzled family from Drosophila functions as a Wingless receptor
    • of special interest. The authors clone a novel Frizzled gene, DFz-2, from Drosophila and provide strong evidence that it acts as a Wg receptor. Transfection of S2 cells with DFz-2 sensitizes these cells to the Wg signal and allows Wg to bind directly to the surface of the cell.
    • 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. of special interest Nature. 382:1996;225-230 The authors clone a novel Frizzled gene, DFz-2, from Drosophila and provide strong evidence that it acts as a Wg receptor. Transfection of S2 cells with DFz-2 sensitizes these cells to the Wg signal and allows Wg to bind directly to the surface of the cell.
    • (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
  • 8
    • 0029781509 scopus 로고    scopus 로고
    • Functional interaction of β-catenin with the transcription factor LEF-1
    • of special interest. The authors use the yeast two-hybrid screen to identify β-catenin interacting proteins and isolate Lef-1. They furthermore demonstrate that β-catenin binding to Lef-1 in a ternary complex with DNA alters Lef-1's ability to bend DNA. Their finding that overexpression of Lef-1 in Xenopus embryos induces a secondary axis is contradictory to results in [9] and suggests a greater complexity in the system than this and other reviews indicate.
    • Behrens J, von Kries JP, Kuhl M, Bruhn L, Wedlich D, Grosschedl R, Birchmeier W. Functional interaction of β-catenin with the transcription factor LEF-1. of special interest Nature. 382:1996;638-642 The authors use the yeast two-hybrid screen to identify β-catenin interacting proteins and isolate Lef-1. They furthermore demonstrate that β-catenin binding to Lef-1 in a ternary complex with DNA alters Lef-1's ability to bend DNA. Their finding that overexpression of Lef-1 in Xenopus embryos induces a secondary axis is contradictory to results in [9] and suggests a greater complexity in the system than this and other reviews indicate.
    • (1996) Nature , vol.382 , pp. 638-642
    • Behrens, J.1    Von Kries, J.P.2    Kuhl, M.3    Bruhn, L.4    Wedlich, D.5    Grosschedl, R.6    Birchmeier, W.7
  • 9
    • 0001003110 scopus 로고    scopus 로고
    • XTcf-3 transcription factor mediates β-catenin-induced axis formation in Xenopus embryos
    • of special interest. The authors isolate several TCF homologs (XTcf-3) from Xenopus and using a two hybrid screen with the amino terminus of human TCF, demonstrate an interaction between β-catenin and TCF. Overexpression of both XTcf-3 and β-catenin results in the nuclear localization of β-catenin. When co-expressed with XTcf-3, β-catenin is able to transactivate a reporter construct containing a TCF/Lef DNA binding motif. Injection of XTcf-3 in Xenopus embryos has no effect on axis formation, an apparent contradiction to the experiments in [8,10]. Deletion of the amino terminus of XTcf-3, the β-catenin interaction domain, blocks β-catenin-induced secondary axis and endogenous axis formation.
    • Molenaar M, van de Wetering M, Oosterwegel M, Peterson-Maduro J, Godsave S, Korinek V, Roose J, Destree O, Clevers H. XTcf-3 transcription factor mediates β-catenin-induced axis formation in Xenopus embryos. of special interest Cell. 86:1996;391-399 The authors isolate several TCF homologs (XTcf-3) from Xenopus and using a two hybrid screen with the amino terminus of human TCF, demonstrate an interaction between β-catenin and TCF. Overexpression of both XTcf-3 and β-catenin results in the nuclear localization of β-catenin. When co-expressed with XTcf-3, β-catenin is able to transactivate a reporter construct containing a TCF/Lef DNA binding motif. Injection of XTcf-3 in Xenopus embryos has no effect on axis formation, an apparent contradiction to the experiments in [8,10]. Deletion of the amino terminus of XTcf-3, the β-catenin interaction domain, blocks β-catenin-induced secondary axis and endogenous axis formation.
    • (1996) Cell , vol.86 , pp. 391-399
    • Molenaar, M.1    Van De Wetering, M.2    Oosterwegel, M.3    Peterson-Maduro, J.4    Godsave, S.5    Korinek, V.6    Roose, J.7    Destree, O.8    Clevers, H.9
  • 10
    • 0345343608 scopus 로고    scopus 로고
    • Nuclear localization of β-catenin by interaction with transcription factor LEF-1
    • of special interest. The authors demonstrate a physical interaction between β-catenin and LEF-1 and show that this complex binds to the promoter region of the E-cadherin gene. In addition, they show that ectopic expression of LEF-1 in Xenopus embryos leads to duplication of the body axis, arguing that LEF-1 overexpression can bypass the need of a Wnt signal input. This result contradicts the findings in [9] which demonstrate that overexpression of XTcf-3 did not cause axis duplication.
    • Huber O, Korn R, McLaughlin J, Ohsugi M, Herrmann BG, Kemler R. Nuclear localization of β-catenin by interaction with transcription factor LEF-1. of special interest Mech Dev. 59:1996;3-10 The authors demonstrate a physical interaction between β-catenin and LEF-1 and show that this complex binds to the promoter region of the E-cadherin gene. In addition, they show that ectopic expression of LEF-1 in Xenopus embryos leads to duplication of the body axis, arguing that LEF-1 overexpression can bypass the need of a Wnt signal input. This result contradicts the findings in [9] which demonstrate that overexpression of XTcf-3 did not cause axis duplication.
    • (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
  • 11
    • 0030999806 scopus 로고    scopus 로고
    • Armadillo coactivates transcription driven by the product of the Drosophila segment polarity gene dTCF
    • of special interest. Using a PCR-based strategy, the authors isolate a TCF homolog from Drosophila, dTCF. Overexpression of a dominant negative dTCF that fails to bind β-catenin and mutants in dTCF produces a segment polarity phenotype. Furthermore, in a dTCF mutant, the effects of a constitutively active arm allele are completely blocked, suggesting that Arm and dTCF interact in vivo. Finally, by fusing the carboxyl terminus of Arm to the Gal-4 DNA-binding domain, the authors demonstrate that this domain of Arm may act as a transcriptional activation domain.
    • Van de Wetering M, Cavallo R, Dooijes D, van Beest M, van Es J, Loureiro J, Ypma A, Hursh D, Jones T, Bejsovec A, et al. Armadillo coactivates transcription driven by the product of the Drosophila segment polarity gene dTCF. of special interest Cell. 88:1997;789-799 Using a PCR-based strategy, the authors isolate a TCF homolog from Drosophila, dTCF. Overexpression of a dominant negative dTCF that fails to bind β-catenin and mutants in dTCF produces a segment polarity phenotype. Furthermore, in a dTCF mutant, the effects of a constitutively active arm allele are completely blocked, suggesting that Arm and dTCF interact in vivo. Finally, by fusing the carboxyl terminus of Arm to the Gal-4 DNA-binding domain, the authors demonstrate that this domain of Arm may act as a transcriptional activation domain.
    • (1997) Cell , vol.88 , pp. 789-799
    • Van De Wetering, M.1    Cavallo, R.2    Dooijes, D.3    Van Beest, M.4    Van Es, J.5    Loureiro, J.6    Ypma, A.7    Hursh, D.8    Jones, T.9    Bejsovec, A.10
  • 12
    • 0031043238 scopus 로고    scopus 로고
    • Pangolin encodes a LEF-1 homologue that acts downstream of armadillo to transduce the Wingless signal in Drosophila
    • of special interest. The authors perform a screen for dominant suppressors of the rough eye phenotype caused by ectopic wingless expression in the Drosophila eye and isolate the LEF-1/TCF homolog pangolin. Besides demonstrating that Pangolin physically interacts with Arm, it is shown that pangolin is required for all assayed wingless signaling events in adult tissues, thus providing in vivo evidence for the role of pangolin in wingless signaling.
    • Brunner E, Peter O, Schweizer L, Basler K. pangolin encodes a LEF-1 homologue that acts downstream of armadillo to transduce the Wingless signal in Drosophila. of special interest Nature. 385:1997;829-833 The authors perform a screen for dominant suppressors of the rough eye phenotype caused by ectopic wingless expression in the Drosophila eye and isolate the LEF-1/TCF homolog pangolin. Besides demonstrating that Pangolin physically interacts with Arm, it is shown that pangolin is required for all assayed wingless signaling events in adult tissues, thus providing in vivo evidence for the role of pangolin in wingless signaling.
    • (1997) Nature , vol.385 , pp. 829-833
    • Brunner, E.1    Peter, O.2    Schweizer, L.3    Basler, K.4
  • 13
    • 0027070855 scopus 로고
    • Wingless signaling acts through zeste-white 3, the Drosophila homolog of glycogen synthase kinase-3, to regulate engrailed and establish cell fate
    • Siegfried E, Chou T, Perrimon N. wingless signaling acts through zeste-white 3, the Drosophila homolog of glycogen synthase kinase-3, to regulate engrailed and establish cell fate. Cell. 71:1992;1167-1179.
    • (1992) Cell , vol.71 , pp. 1167-1179
    • Siegfried, E.1    Chou, T.2    Perrimon, N.3
  • 14
    • 0027948042 scopus 로고
    • Components of wingless signaling in Drosophila
    • Siegfried E, Wilder E, Perrimon N. Components of wingless signaling in Drosophila. Nature. 367:1994;76-80.
    • (1994) Nature , vol.367 , pp. 76-80
    • Siegfried, E.1    Wilder, E.2    Perrimon, N.3
  • 15
    • 0028176875 scopus 로고
    • Dishevelled and armadillo act in the wingless signaling pathway in Drosophila
    • Noordermeer J, Klingensmith J, Perrimon N, Nusse R. dishevelled and armadillo act in the wingless signaling pathway in Drosophila. Nature. 367:1994;80-83.
    • (1994) Nature , vol.367 , pp. 80-83
    • Noordermeer, J.1    Klingensmith, J.2    Perrimon, N.3    Nusse, R.4
  • 16
    • 0029811434 scopus 로고    scopus 로고
    • Wingless inactivates glycogen synthase kinase-3 via an intracellular signalling pathway which involves a protein kinase C
    • Cook D, Fry MJ, Hughes K, Sumathipala R, Woodgett JR, Dale TC. Wingless inactivates glycogen synthase kinase-3 via an intracellular signalling pathway which involves a protein kinase C. EMBO J. 15:1996;4526-4536.
    • (1996) EMBO J , vol.15 , pp. 4526-4536
    • Cook, D.1    Fry, M.J.2    Hughes, K.3    Sumathipala, R.4    Woodgett, J.R.5    Dale, T.C.6
  • 17
    • 23444459214 scopus 로고
    • Biological activity of soluble Wingless protein in cultured imaginal disc cells
    • Van Leeuwen F, Samos CH, Nusse R. Biological activity of soluble Wingless protein in cultured imaginal disc cells. Nature. 368:1994;342-344.
    • (1994) Nature , vol.368 , pp. 342-344
    • Van Leeuwen, F.1    Samos, C.H.2    Nusse, R.3
  • 18
    • 0028266975 scopus 로고
    • A repeating amino acid motif shared by proteins with diverse cellular roles (Letter)
    • Peifer M, Berg S, Reynolds AB. A repeating amino acid motif shared by proteins with diverse cellular roles (Letter). Cell. 76:1994;789-791.
    • (1994) Cell , vol.76 , pp. 789-791
    • Peifer, M.1    Berg, S.2    Reynolds, A.B.3
  • 19
    • 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
    • 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. 10:1996;1443-1454.
    • (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
  • 20
    • 0029898417 scopus 로고    scopus 로고
    • Deletion of an amino-terminal sequence β-catenin in vivo and promotes hyperphosphorylation of the adenomatous polyposis coli tumor suppressor protein
    • Munemitsu S, Albert I, Rubinfeld B, Polakis P. Deletion of an amino-terminal sequence β-catenin in vivo and promotes hyperphosphorylation of the adenomatous polyposis coli tumor suppressor protein. Mol Cell Biol. 16:1996;4088-4094.
    • (1996) Mol Cell Biol , vol.16 , pp. 4088-4094
    • Munemitsu, S.1    Albert, I.2    Rubinfeld, B.3    Polakis, P.4
  • 21
    • 0030614352 scopus 로고    scopus 로고
    • NH2-terminal deletion of β-catenin results in stable colocalization of mutant β-catenin with adenomatous polyposis coli protein and altered MDCK cell adhesion
    • Barth AI, Pollack AL, Altschuler Y, Mostov KE, Nelson WJ. NH2-terminal deletion of β-catenin results in stable colocalization of mutant β-catenin with adenomatous polyposis coli protein and altered MDCK cell adhesion. J Cell Biol. 136:1997;693-706.
    • (1997) J Cell Biol , vol.136 , pp. 693-706
    • Barth, A.I.1    Pollack, A.L.2    Altschuler, Y.3    Mostov, K.E.4    Nelson, W.J.5
  • 22
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of β-catenin
    • of outstanding interest. This paper describes the three-dimensional structure of the arm repeat region of β-catenin. The final structure is a tightly packed series of interacting α-helices that form a rigid right-handed superhelix. A shallow groove with an overall basic charge is likely to represent the protein-binding surface on β-catenin that interacts with E-cadherin, APC and TCF.
    • Huber A, Nelson J, Weiss W. Three-dimensional structure of the armadillo repeat region of β-catenin. of outstanding interest Cell. 90:1997;871-882 This paper describes the three-dimensional structure of the arm repeat region of β-catenin. The final structure is a tightly packed series of interacting α-helices that form a rigid right-handed superhelix. A shallow groove with an overall basic charge is likely to represent the protein-binding surface on β-catenin that interacts with E-cadherin, APC and TCF.
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.1    Nelson, J.2    Weiss, W.3
  • 23
    • 0028572556 scopus 로고
    • E-cadherin and APC compete for the interaction with β-catenin and the cytoskeleton
    • Huelsken J, Birchmeier W, Behrens J. E-cadherin and APC compete for the interaction with β-catenin and the cytoskeleton. J Cell Biol. 127:1994;2061-2069.
    • (1994) J Cell Biol , vol.127 , pp. 2061-2069
    • Huelsken, J.1    Birchmeier, W.2    Behrens, J.3
  • 24
    • 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. 270:1995;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
  • 26
    • 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
    • of special interest. This paper presents a very thorough in vivo mutational analysis of arm in Drosophila. Among this vast amount of data is an experiment in which two embryonic lethal alleles of arm - one being defective in Wg signaling and the other being defective in cell adhesion - complement each other, thus demonstrating that the functions of Arm in Wg signaling and cell adhesion are truly separable and independent. One mutant Arm protein, which does not interact with dTCF and is inactive in Wg signaling, still localizes to the nucleus, thus arguing that a mechanism not involving dTCF is required for Arm's nuclear localization.
    • Orsulic S, Peifer M. 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. of special interest J Cell Biol. 134:1996;1283-1300 This paper presents a very thorough in vivo mutational analysis of arm in Drosophila. Among this vast amount of data is an experiment in which two embryonic lethal alleles of arm - one being defective in Wg signaling and the other being defective in cell adhesion - complement each other, thus demonstrating that the functions of Arm in Wg signaling and cell adhesion are truly separable and independent. One mutant Arm protein, which does not interact with dTCF and is inactive in Wg signaling, still localizes to the nucleus, thus arguing that a mechanism not involving dTCF is required for Arm's nuclear localization.
    • (1996) J Cell Biol , vol.134 , pp. 1283-1300
    • Orsulic, S.1    Peifer, M.2
  • 27
    • 0029776445 scopus 로고    scopus 로고
    • β-catenin associates with the actin-bundling protein fascin in a noncadherin complex
    • Tao YS, Edwards RA, Tubb B, Wang S, Bryan J, McCrea PD. β-catenin associates with the actin-bundling protein fascin in a noncadherin complex. J Cell Biol. 134:1996;1271-1281.
    • (1996) J Cell Biol , vol.134 , pp. 1271-1281
    • Tao, Y.S.1    Edwards, R.A.2    Tubb, B.3    Wang, S.4    Bryan, J.5    McCrea, P.D.6
  • 28
    • 0029664368 scopus 로고    scopus 로고
    • Binding of GSK3β to the APC-β-catenin complex and regulation of complex assembly
    • When complexed with β-catenin, APC also associates with GSK3, another component of the Wnt signaling pathway. GSK3 phosphorylates APC in vitro and this phosphorylation greatly enhances the binding of β-catenin to APC.
    • Rubinfeld B, Albert I, Porfiri E, Fiol C, Munemitsu S, Polakis P. Binding of GSK3β to the APC-β-catenin complex and regulation of complex assembly. Science. 272:1996;1023-1026 When complexed with β-catenin, APC also associates with GSK3, another component of the Wnt signaling pathway. GSK3 phosphorylates APC in vitro and this phosphorylation greatly enhances the binding of β-catenin to APC.
    • (1996) Science , vol.272 , pp. 1023-1026
    • Rubinfeld, B.1    Albert, I.2    Porfiri, E.3    Fiol, C.4    Munemitsu, S.5    Polakis, P.6
  • 29
    • 0030844356 scopus 로고    scopus 로고
    • Negative regulation of armadillo, a wingless effector in Drosophila
    • of special interest. The authors characterize an arm allele lacking 54 amino acids in its amino terminus and show that it is constitutively active in Wg signaling. This allele is still phosphorylated even in a zw3 mutant background, suggesting that additional kinases other than Zw3 are involved in its phosphorylation.
    • Pai LM, Orsulic S, Bejsovec A, Peifer M. Negative regulation of armadillo, a wingless effector in Drosophila. of special interest Development. 124:1997;2255-2266 The authors characterize an arm allele lacking 54 amino acids in its amino terminus and show that it is constitutively active in Wg signaling. This allele is still phosphorylated even in a zw3 mutant background, suggesting that additional kinases other than Zw3 are involved in its phosphorylation.
    • (1997) Development , vol.124 , pp. 2255-2266
    • Pai, L.M.1    Orsulic, S.2    Bejsovec, A.3    Peifer, M.4
  • 30
    • 0030978351 scopus 로고    scopus 로고
    • β-catenin is a target for the ubiquitin-proteasome pathway
    • of special interest. This paper demonstrates that β-catenin is degraded by the ubiquitin-proteasome pathway. Mutation of putative phosphorylation sites (speculated GSK3 phosphorylation sites) stabilizes β-catenin and blocks ubiquitination. A remaining issue is whether phosphorylation at these sites is a prerequisite for degradation by the ubiquitin-proteasome pathway.
    • Aberle H, Bauer A, Stappert J, Kispert A, Kemler R. β-catenin is a target for the ubiquitin-proteasome pathway. of special interest EMBO J. 16:1997;3797-3804 This paper demonstrates that β-catenin is degraded by the ubiquitin-proteasome pathway. Mutation of putative phosphorylation sites (speculated GSK3 phosphorylation sites) stabilizes β-catenin and blocks ubiquitination. A remaining issue is whether phosphorylation at these sites is a prerequisite for degradation by the ubiquitin-proteasome pathway.
    • (1997) EMBO J , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 31
    • 0030949463 scopus 로고    scopus 로고
    • Activation of β-catenin-Tcf signaling in colon cancer by mutations in β-catenin or APC
    • of special interest. Certain colorectal tumor cell lines contain mutations in β-catenin that render the β-catenin protein insensitive to APC-mediated destabilization. Many of the mutations in β-catenin are in serine residues which are implicated in downregulation of β-catenin by GSK3 phosphorylation. These cell lines contain constitutive β-catenin/TCF-regulated transcription which was not inhibited by exogenous APC.
    • Morin PJ, Sparks AB, Korinek V, Barker N, Clevers H, Vogelstein B, Kinzler KW. Activation of β-catenin-Tcf signaling in colon cancer by mutations in β-catenin or APC. of special interest Science. 275:1997;1787-1790 Certain colorectal tumor cell lines contain mutations in β-catenin that render the β-catenin protein insensitive to APC-mediated destabilization. Many of the mutations in β-catenin are in serine residues which are implicated in downregulation of β-catenin by GSK3 phosphorylation. These cell lines contain constitutive β-catenin/TCF-regulated transcription which was not inhibited by exogenous APC.
    • (1997) Science , vol.275 , pp. 1787-1790
    • Morin, P.J.1    Sparks, A.B.2    Korinek, V.3    Barker, N.4    Clevers, H.5    Vogelstein, B.6    Kinzler, K.W.7
  • 32
    • 0030900696 scopus 로고    scopus 로고
    • Stabilization of β-catenin by genetic defects in melanoma cell lines
    • of special interest. In this paper, the authors demonstrate that a number of human melanoma cell lines contained elevated levels of β-catenin. This increase was attributed to mutations in the β-catenin gene that result in the stabilization of the protein and to mutations in APC. Elevated levels of β-catenin also correlated with the presence of a constitutive β-catenin/LEF-1 complex. Interestingly, several of the mutations in β-catenin, that resulted in increased stability of the protein, changed conserved serine residues in the amino terminus, a finding that along with other data suggests that these residues are phosphorylated and that this phosphorylation is involved in the destabilization of β-catenin.
    • Rubinfeld B, Robbins P, El-Gamil M, Albert I, Porfiri E, Polakis P. Stabilization of β-catenin by genetic defects in melanoma cell lines. of special interest Science. 275:1997;1790-1792 In this paper, the authors demonstrate that a number of human melanoma cell lines contained elevated levels of β-catenin. This increase was attributed to mutations in the β-catenin gene that result in the stabilization of the protein and to mutations in APC. Elevated levels of β-catenin also correlated with the presence of a constitutive β-catenin/LEF-1 complex. Interestingly, several of the mutations in β-catenin, that resulted in increased stability of the protein, changed conserved serine residues in the amino terminus, a finding that along with other data suggests that these residues are phosphorylated and that this phosphorylation is involved in the destabilization of β-catenin.
    • (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
  • 33
    • 0031557898 scopus 로고    scopus 로고
    • The adenomatous polyposis coli (APC) tumor suppressor
    • of special interest. A comprehensive review of the literature on APC.
    • Polakis P. The adenomatous polyposis coli (APC) tumor suppressor. of special interest Biochim Biophys Acta. 1332:1997;F127-F147 A comprehensive review of the literature on APC.
    • (1997) Biochim Biophys Acta , vol.1332
    • Polakis, P.1
  • 34
    • 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. 92:1995;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
  • 35
    • 0031013879 scopus 로고    scopus 로고
    • A Drosophila homolog of the tumor suppressor gene adenomatous polyposis coli down-regulates β-catenin but its zygotic expression is not essential for the regulation of Armadillo
    • of outstanding interest. of special interest. By screening a Drosophila expression library with an antibody against human APC, the authors isolate an APC homolog, called D-APC. Even though D-APC interacts directly with Arm in vitro and reduces β-catenin levels when overexpressed in cells lacking wild-type APC, removal of zygotic D-APC did not alter Arm protein distribution and no phenotypes suggesting an inhibitory role in Wg signaling were observed. These results, in combination with the results in C. elegans [37] and the results in Xenopus [36], suggest a more complex function for APC in Wnt signaling than was previously thought.
    • of outstanding interest Hayashi S, Rubinfeld B, Souza B, Polakis P, Wieschaus E, Levine AJ. A Drosophila homolog of the tumor suppressor gene adenomatous polyposis coli down-regulates β-catenin but its zygotic expression is not essential for the regulation of Armadillo. of special interest Proc Natl Acad Sci USA. 94:1997;242-247 By screening a Drosophila expression library with an antibody against human APC, the authors isolate an APC homolog, called D-APC. Even though D-APC interacts directly with Arm in vitro and reduces β-catenin levels when overexpressed in cells lacking wild-type APC, removal of zygotic D-APC did not alter Arm protein distribution and no phenotypes suggesting an inhibitory role in Wg signaling were observed. These results, in combination with the results in C. elegans [37] and the results in Xenopus [36], suggest a more complex function for APC in Wnt signaling than was previously thought.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 242-247
    • Hayashi, S.1    Rubinfeld, B.2    Souza, B.3    Polakis, P.4    Wieschaus, E.5    Levine, A.J.6
  • 36
    • 0031058705 scopus 로고    scopus 로고
    • Adenomatous polyposis coli tumor suppressor protein has signaling activity in Xenopus laevis embryos resulting in the induction of an ectopic dorsoanterior axis
    • of outstanding interest. of special interest. Ectopic expression of APC in Xenopus embryos induces a secondary axis, suggesting a positive rather than a negative role for APC in Wnt signaling. This axis induction by APC is dependent on the availability of free β-catenin. These results in conjunction with the work in [37] suggest a more complex role for APC in the Wnt signaling pathway than simply targeting β-catenin for degradation.
    • of outstanding interest Vleminckx K, Wong E, Guger K, Rubinfeld B, Polakis P, Gumbiner BM. Adenomatous polyposis coli tumor suppressor protein has signaling activity in Xenopus laevis embryos resulting in the induction of an ectopic dorsoanterior axis. of special interest J Cell Biol. 136:1997;411-420 Ectopic expression of APC in Xenopus embryos induces a secondary axis, suggesting a positive rather than a negative role for APC in Wnt signaling. This axis induction by APC is dependent on the availability of free β-catenin. These results in conjunction with the work in [37] suggest a more complex role for APC in the Wnt signaling pathway than simply targeting β-catenin for degradation.
    • (1997) J Cell Biol , vol.136 , pp. 411-420
    • Vleminckx, K.1    Wong, E.2    Guger, K.3    Rubinfeld, B.4    Polakis, P.5    Gumbiner, B.M.6
  • 37
    • 0030829387 scopus 로고    scopus 로고
    • Wnt signaling and an APC-related gene specify endoderm in early C. elegans embryos
    • of outstanding interest. The authors use both a genetic screen and an RNA-mediated interference (RNA) technique to identify genes involved in the specification of endoderm in early C. elegans embryos. The genes described are related to wnt/wingless (mom-2), porcupine (mom-1), frizzled (mom-5), β-catenin/armadillo (wrm-1), and APC (apr-1), all of which have been implicated in the transduction of the Wnt signal in other systems. Unlike in previously studied systems, wrm-1 acts to inhibit the activity of pop-1, a TCF homolog, presumably by facilitating the movement of POP-1 out of the nucleus. Several of these so-called mom mutants also display an abnormal orientation of certain mitotic spindles. pop-1 mutants do not display this effect, thus suggesting that the Wnt signaling pathway affects spindle orientation in a pop-1 independent pathway.
    • Rocheleau C, Downs W, Lin R, Wittmann C, Bei Y, Cha Y-H, Ali M, Priess J, Mello C. Wnt signaling and an APC-related gene specify endoderm in early C. elegans embryos. of outstanding interest Cell. 90:1997;707-716 The authors use both a genetic screen and an RNA-mediated interference (RNA) technique to identify genes involved in the specification of endoderm in early C. elegans embryos. The genes described are related to wnt/wingless (mom-2), porcupine (mom-1), frizzled (mom-5), β-catenin/armadillo (wrm-1), and APC (apr-1), all of which have been implicated in the transduction of the Wnt signal in other systems. Unlike in previously studied systems, wrm-1 acts to inhibit the activity of pop-1, a TCF homolog, presumably by facilitating the movement of POP-1 out of the nucleus. Several of these so-called mom mutants also display an abnormal orientation of certain mitotic spindles. pop-1 mutants do not display this effect, thus suggesting that the Wnt signaling pathway affects spindle orientation in a pop-1 independent pathway.
    • (1997) Cell , vol.90 , pp. 707-716
    • Rocheleau, C.1    Downs, W.2    Lin, R.3    Wittmann, C.4    Bei, Y.5    Cha Y-H6    Ali, M.7    Priess, J.8    Mello, C.9
  • 38
    • 0030861128 scopus 로고    scopus 로고
    • Analysis of the signaling activities of localization mutants of β-catenin during axis specification in Xenopus
    • of special interest. A membrane-tethered β-catenin is still able to induce a secondary axis in Xenopus even though it fails to enter the nucleus itself. The authors argue that overexpression of this mislocalized β-catenin competes with the endogenous degradation machinery thus permitting accumulation and subsequent nuclear entry of the endogenous β-catenin.
    • Miller J, Moon R. Analysis of the signaling activities of localization mutants of β-catenin during axis specification in Xenopus. of special interest J Cell Biol. 139:1997;229-243 A membrane-tethered β-catenin is still able to induce a secondary axis in Xenopus even though it fails to enter the nucleus itself. The authors argue that overexpression of this mislocalized β-catenin competes with the endogenous degradation machinery thus permitting accumulation and subsequent nuclear entry of the endogenous β-catenin.
    • (1997) J Cell Biol , vol.139 , pp. 229-243
    • Miller, J.1    Moon, R.2
  • 39
    • 0028954815 scopus 로고
    • Embryonic axis induction by the armadillo repeat domain of β-catenin: Evidence for intracellular signaling
    • Funayama N, Fagotto F, McCrea P, Gumbiner BM. Embryonic axis induction by the armadillo repeat domain of β-catenin: evidence for intracellular signaling. J Cell Biol. 128:1995;959-968.
    • (1995) J Cell Biol , vol.128 , pp. 959-968
    • Funayama, N.1    Fagotto, F.2    McCrea, P.3    Gumbiner, B.M.4
  • 40
    • 0025605601 scopus 로고
    • The segment polarity gene armadillo encodes a functionally modular protein that is the Drosophila homolog of human plakoglobin
    • Peifer M, Wieschaus E. The segment polarity gene armadillo encodes a functionally modular protein that is the Drosophila homolog of human plakoglobin. Cell. 63:1990;1167-1176.
    • (1990) Cell , vol.63 , pp. 1167-1176
    • Peifer, M.1    Wieschaus, E.2
  • 41
    • 0030979996 scopus 로고    scopus 로고
    • LEF-1, a nuclear factor coordinating signaling inputs from wingless and decapentaplegic
    • of special interest. LEF-1 activates transcription of Ubx in the midgut by binding to a TCF-binding site in the Wingless-responsive element of the Ubx promoter. Arm forms a stable ternary complex with LEF-1 and DNA and is required for LEF-1-dependent activation. Overexpression of LEF-1 displays similar phenotypes as ubiquitously expressed wingless, demonstrating that LEF-1 overexpression bypasses the Wingless signal. Furthermore, wingless and decapentaplegic signaling work synergistically to affect this process.
    • Riese J, Yu X, Munnerlyn A, Eresh S, Hsu S-C, Grosschedl R, Bienz M. LEF-1, a nuclear factor coordinating signaling inputs from wingless and decapentaplegic. of special interest Cell. 88:1997;777-787 LEF-1 activates transcription of Ubx in the midgut by binding to a TCF-binding site in the Wingless-responsive element of the Ubx promoter. Arm forms a stable ternary complex with LEF-1 and DNA and is required for LEF-1-dependent activation. Overexpression of LEF-1 displays similar phenotypes as ubiquitously expressed wingless, demonstrating that LEF-1 overexpression bypasses the Wingless signal. Furthermore, wingless and decapentaplegic signaling work synergistically to affect this process.
    • (1997) Cell , vol.88 , pp. 777-787
    • Riese, J.1    Yu, X.2    Munnerlyn, A.3    Eresh, S.4    Hsu S-C5    Grosschedl, R.6    Bienz, M.7
  • 42
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear import
    • Goerlich D, Prehn S, Laskey RA, Harmann E. Isolation of a protein that is essential for the first step of nuclear import. Cell. 79:1994;767-778.
    • (1994) Cell , vol.79 , pp. 767-778
    • Goerlich, D.1    Prehn, S.2    Laskey, R.A.3    Harmann, E.4
  • 43
    • 0030899553 scopus 로고    scopus 로고
    • Establishment of the dorso-ventral axis in Xenopus embryos is presaged by early asymmetries in beta-catenin that are modulated by the Wnt signaling pathway
    • of special interest. By careful confocal microscopy, the authors argue that at the two cell stage more cytoplasmic β-catenin has accumulated on the future dorsal side of the Xenopus embryo. By later stages, β-catenin accumulates in dorsal but not ventral nuclei. Based on these results, the authors suggest that β-catenin asymmetries presage and may specify dorsal-ventral differences in gene expression.
    • Larabell CA, Torres M, Rowning BA, Yost C, Miller JR, Wu M, Kimelman D, Moon RT. Establishment of the dorso-ventral axis in Xenopus embryos is presaged by early asymmetries in beta-catenin that are modulated by the Wnt signaling pathway. of special interest J Cell Biol. 136:1997;1123-1136 By careful confocal microscopy, the authors argue that at the two cell stage more cytoplasmic β-catenin has accumulated on the future dorsal side of the Xenopus embryo. By later stages, β-catenin accumulates in dorsal but not ventral nuclei. Based on these results, the authors suggest that β-catenin asymmetries presage and may specify dorsal-ventral differences in gene expression.
    • (1997) J Cell Biol , vol.136 , pp. 1123-1136
    • Larabell, C.A.1    Torres, M.2    Rowning, B.A.3    Yost, C.4    Miller, J.R.5    Wu, M.6    Kimelman, D.7    Moon, R.T.8
  • 44
    • 0030930442 scopus 로고    scopus 로고
    • A β-catenin/XTcf-3 complex binds to the Siamois promoter to regulate dorsal axis specification in Xenopus
    • of outstanding interest. The promoter of the dorsalizing homeobox gene siamois in Xenopus is shown to be a direct target of the β-catenin/XTCF-3 complex, thus establishing a link between the Wnt pathway and the activation of genes involved in specifying the dorsal axis. The authors also demonstrate that XTCF-3 in the absence of β-catenin, and hence in the absence of a Wnt signal, can act as a transcriptional repressor. The dorsal activation in combination with ventral repression of the siamois promoter is hypothesized to result in a very restricted pattern of siamois expression.
    • Brannon M, Gomperts M, Sumoy L, Moon R, Kimelman D. A β-catenin/XTcf-3 complex binds to the Siamois promoter to regulate dorsal axis specification in Xenopus. of outstanding interest Genes Dev. 11:1997;2359-2370 The promoter of the dorsalizing homeobox gene siamois in Xenopus is shown to be a direct target of the β-catenin/XTCF-3 complex, thus establishing a link between the Wnt pathway and the activation of genes involved in specifying the dorsal axis. The authors also demonstrate that XTCF-3 in the absence of β-catenin, and hence in the absence of a Wnt signal, can act as a transcriptional repressor. The dorsal activation in combination with ventral repression of the siamois promoter is hypothesized to result in a very restricted pattern of siamois expression.
    • (1997) Genes Dev , vol.11 , pp. 2359-2370
    • Brannon, M.1    Gomperts, M.2    Sumoy, L.3    Moon, R.4    Kimelman, D.5
  • 45
    • 0028986250 scopus 로고
    • Assembly and function of a TCRα enhancer complex is dependant on LEF-1-induced DNA bending and multiple protein-protein interactions
    • Giese K, Kingsley C, Kirshner JR, Grosschedl R. Assembly and function of a TCRα enhancer complex is dependant on LEF-1-induced DNA bending and multiple protein-protein interactions. Genes Dev. 9:1995;995-1008.
    • (1995) Genes Dev , vol.9 , pp. 995-1008
    • Giese, K.1    Kingsley, C.2    Kirshner, J.R.3    Grosschedl, R.4
  • 46
    • 0030747773 scopus 로고    scopus 로고
    • Wnt signaling polarizes an early C. elegans blastomere to distinguish endoderm from mesoderm
    • of outstanding interest. In a genetic screen in C. elegans for mutants that produce more mesoderm at the expense of endoderm, the authors identify five genes, mom-1 through mom-5. mom-2 encodes a Wnt protein which signals to a neighboring cell to adopt an endoderm fate. In mom-2 mutants, POP-1 - a TCF-related protein, which normally is at relatively low levels in the nucleus of this neighboring cell - accumulates to higher levels, suggesting that mom-2's role is to reduce nuclear levels of POP-1. This result contradicts findings in other systems where TCF is thought to be activated by Wnt signaling. The authors furthermore characterize a mitotic spindle defect in mom mutants and suggest that Wnt signaling regulates cytoskeletal polarity.
    • Thorpe CJ, Schlesinger A, Carter JC, Bowerman B. Wnt signaling polarizes an early C. elegans blastomere to distinguish endoderm from mesoderm. of outstanding interest Cell. 90:1997;695-705 In a genetic screen in C. elegans for mutants that produce more mesoderm at the expense of endoderm, the authors identify five genes, mom-1 through mom-5. mom-2 encodes a Wnt protein which signals to a neighboring cell to adopt an endoderm fate. In mom-2 mutants, POP-1 - a TCF-related protein, which normally is at relatively low levels in the nucleus of this neighboring cell - accumulates to higher levels, suggesting that mom-2's role is to reduce nuclear levels of POP-1. This result contradicts findings in other systems where TCF is thought to be activated by Wnt signaling. The authors furthermore characterize a mitotic spindle defect in mom mutants and suggest that Wnt signaling regulates cytoskeletal polarity.
    • (1997) Cell , vol.90 , pp. 695-705
    • Thorpe, C.J.1    Schlesinger, A.2    Carter, J.C.3    Bowerman, B.4
  • 47
    • 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. 83:1995;599-609.
    • (1995) Cell , vol.83 , pp. 599-609
    • Lin, R.1    Thompson, S.2    Priess, J.R.3
  • 48
    • 0029417002 scopus 로고
    • Dishevelled is a component of the frizzled signaling pathway in Drosophila
    • Krasnow RE, Wong LL, Adler PN. Dishevelled is a component of the frizzled signaling pathway in Drosophila. Development. 121:1995;4095-4102.
    • (1995) Development , vol.121 , pp. 4095-4102
    • Krasnow, R.E.1    Wong, L.L.2    Adler, P.N.3
  • 49
    • 0030917227 scopus 로고    scopus 로고
    • The role of RhoA in tissue polarity and Frizzled signaling
    • of special interest. The authors demonstrate that hypomorphic alleles of RhoA p21 GTPase give rise to phenotypes that are very similar to those of tissue polarity mutants, namely frizzled and dsh. Genetic evidence is provided that JNK/SAPK-like kinases act in the Fz/RhoA-mediated polarity signaling. This pathway may represent a novel Wnt pathway that does not involve Arm and TCF.
    • Strutt DI, Weber U, Mlodzik M. The role of RhoA in tissue polarity and Frizzled signaling. of special interest Nature. 387:1997;292-295 The authors demonstrate that hypomorphic alleles of RhoA p21 GTPase give rise to phenotypes that are very similar to those of tissue polarity mutants, namely frizzled and dsh. Genetic evidence is provided that JNK/SAPK-like kinases act in the Fz/RhoA-mediated polarity signaling. This pathway may represent a novel Wnt pathway that does not involve Arm and TCF.
    • (1997) Nature , vol.387 , pp. 292-295
    • Strutt, D.I.1    Weber, U.2    Mlodzik, M.3
  • 50
    • 0030771851 scopus 로고    scopus 로고
    • Accumulation of Armadillo induced by Wingless, Dishevelled, and dominant negative Zeste-white 3 leads to elevated DE-cadherin in Drosophila Clone 8 wing disc cells
    • of special interest. Activation of the Wingless pathway in Drosophila cell culture by overexpression of dsh or dominant negative zeste-white 3 leads to the transcriptional activation of the DE-cadherin gene. The authors speculate that DE-cadherin is a direct transcriptional target of the β-catenin/Arm-TCF complex and hence of the Wnt pathway. These results demonstrate that Wingless signaling, at least indirectly, can modulate cell adhesion.
    • Yanagawa S, Lee J-S, Haruna T, Oda H, Uemura T, Takeichi M, Ishimoto A. Accumulation of Armadillo induced by Wingless, Dishevelled, and dominant negative Zeste-white 3 leads to elevated DE-cadherin in Drosophila Clone 8 wing disc cells. of special interest J Biol Chem. 272:1997;25243-25251 Activation of the Wingless pathway in Drosophila cell culture by overexpression of dsh or dominant negative zeste-white 3 leads to the transcriptional activation of the DE-cadherin gene. The authors speculate that DE-cadherin is a direct transcriptional target of the β-catenin/Arm-TCF complex and hence of the Wnt pathway. These results demonstrate that Wingless signaling, at least indirectly, can modulate cell adhesion.
    • (1997) J Biol Chem , vol.272 , pp. 25243-25251
    • Yanagawa, S.1    Lee J-S2    Haruna, T.3    Oda, H.4    Uemura, T.5    Takeichi, M.6    Ishimoto, A.7
  • 51
    • 0029915306 scopus 로고    scopus 로고
    • Binding to cadherins antagonizes the signaling activity of β-catenin during axis formation in Xenopus
    • Fagotto F, Funayama N, Gluck U, Gumbiner BM. Binding to cadherins antagonizes the signaling activity of β-catenin during axis formation in Xenopus. J Cell Biol. 132:1996;1105-1114.
    • (1996) J Cell Biol , vol.132 , pp. 1105-1114
    • Fagotto, F.1    Funayama, N.2    Gluck, U.3    Gumbiner, B.M.4


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