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Volumn 7, Issue 4, 1997, Pages 459-466

Armadillo and dTCF: A marriage made in the nucleus

Author keywords

[No Author keywords available]

Indexed keywords

BETA CATENIN; DNA BINDING PROTEIN; HIGH MOBILITY GROUP PROTEIN; TRANSCRIPTION FACTOR;

EID: 0030870391     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(97)80071-8     Document Type: Article
Times cited : (77)

References (68)
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    • Negative regulation of Armadillo, a Wingless effector in Drosophila
    • of special interest. An in vivo demonstration that deletion of the amino-terminal 54 residues of Armadillo yields a protein that has escaped zw3 negative regulation and is constitutively active in Wingless signaling. Multiple phosphoisoforms of this amino-terminally deleted Armadillo are identified, demonstrating the existence of Armadillo phosphorylation sites in regions other than the amino terminus.
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    • β-catenin is a target for the ubiquitin-proteasome pathway
    • of special interest. The authors demonstrate that first, β-catenin is ubiquitinated; second, that ubiquitination requires an intact GSK phosphorylation site in β-catenin; and third, that ubiquitination of β-atenin is inhibited in Wnt-expressing cells; therefore, it is suggested that β-catenin degradation occurs via the ubiquitin-proteasome pathway.
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    • of special interest. Co-immunoprecipitation studies used to demonstrate first, that GSK binding to APC is promoted in the presence of excess β-catenin; second, that GSK phosphorylates the central region of APC in vitro; and third, that GSK phosphorylation of the central region of APC promotes the binding of β-catenin to this region of APC. A potential mechanism for GSK-mediated regulation of Wingless/Wnt signaling may be to promote binding of β-catenin to APC, with the consequences being that β-catenin is targeted for degradation.
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    • of special interest. This paper reports the cloning and sequencing of a Drosophila APC homolog. Zygotic dAPC null mutant embryos show normal Armadillo stripe patterns and essentially normal ventral cuticle morphology, suggesting that zygotic dAPC does not contribute to Armadillo regulation during early embryonic cuticle patterning. APC accumulates to high levels in the CNS and mutants have a CNS phenotype.
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    • of special interest. Removal of both zygotic and maternally contributed armadillo causes defective adherens junction assembly, defective cell adhesion, and alterations in overall cell polarity and in the polarity of the actin cytoskeleton, with drastic consequences for embryonic development at the point of gastrulation. Both maternally- and zygotically-contributed Armadillo, therefore, have roles in embryonic epithelial adhesion and cell fate determination.
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    • of special interest. Immunoprecipitation studies are used to demonstrate an association between Receptor PTPμ and the β-catenin/cadherin complex. PTPμ may thus regulate the state of phosphorylation of the β-catenin/cadherin complex.
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    • Regulated binding of a PTB1B-like phosphatase to N-cadherin: Control of cadherin-mediated adhesion by dephosphorylation of β-catenin
    • of special interest. Demonstration that N-cadherin directly to the phosphatase PTP1B-LP and that this binding is dependent upon tyrosine phosphorylation of PTP1B-LP. Additionally, the authors demonstrate that β-catenin contains no phosphotyrosine when associated with N-cadherin in chick retina. The authors suggest that the binding and phosphatase activity of PTP1B-LP may regulate β-catenin's association with N-cadherin.
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    • Lack of association between receptor protein tyrosine phosphatase RPTP mu and cadherins
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    • β-catenin associates with the actin-bundling protein fascin in a non-cadherin complex
    • of special interest. The yeast two-hybrid system, co-immunoprecipitation experiments, and in vitro binding studies are used to show that the actin bundling protein fascin binds to the central Armadillo repeat domain of β-catenin. Immunofluorescence studies demonstrate the co-localization of fascin and β-catenin at cell - cell borders and cell leading edges, suggesting a role for β-catenin in the regulation of cell motility.
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    • The Adenomatous Polyposis Coli (APC) tumor suppressor protein localizes to plasma membrane sites involved in active cell migration
    • of special interest. APC is shown to co-localize with microtubules in regions of actively migrating cell membranes, suggesting a role for APC in the regulation of directed cell migration.
    • Nüthke IS, Adams CL, Polakis P, Sellin JH, Nelson WJ. The Adenomatous Polyposis Coli (APC) tumor suppressor protein localizes to plasma membrane sites involved in active cell migration. of special interest J Cell Biol. 134:1996;165-180 APC is shown to co-localize with microtubules in regions of actively migrating cell membranes, suggesting a role for APC in the regulation of directed cell migration.
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    • Amino-terminal deletion of β-catenin results in stable co-localization of mutant β-catenin with APC protein and altered MDCK cell adhesion
    • of special interest. Deletion of the amino terminus stabilizes β-catenin when bound to APC. Additionally, amino-terminally deleted β-catenin co-localizes with APC in clusters at the tips of plasma membrane protrusions; whereas full-length β-catenin co-localizes with APC much less dramatically. MDCK cells expressing amino-terminally deleted β-catenin form less compact cell colonies. The authors suggest that the binding of β-catenin to APC regulates APC's role in cell migration
    • Barth AIM, Pollack AL, Altschuler Y, Mostov KE, Nelson WJ. Amino-terminal deletion of β-catenin results in stable co-localization of mutant β-catenin with APC protein and altered MDCK cell adhesion. of special interest J Cell Biol. 136:1997;693-706 Deletion of the amino terminus stabilizes β-catenin when bound to APC. Additionally, amino-terminally deleted β-catenin co-localizes with APC in clusters at the tips of plasma membrane protrusions; whereas full-length β-catenin co-localizes with APC much less dramatically. MDCK cells expressing amino-terminally deleted β-catenin form less compact cell colonies. The authors suggest that the binding of β-catenin to APC regulates APC's role in cell migration.
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    • Dynamics of β-catenin interactions with APC protein regulate epithelial tubulogenesis
    • of special interest. Expression of amino-terminally deleted β-catenin in MDCK epithelial cells inhibits formation of cell extensions and tubule development in an in vitro tubulogenesis assay, indicating that β-catenin and β-catenin/APC interactions regulate epithelial cell migration. Cells expressing amino-terminally deleted β-catenin form aggregates that the authors note mimic the appearance of APC mutant colon polyps.
    • Pollack AL, Barth AIM, Altschuler Y, Nelson WJ, Mostov KE. Dynamics of β-catenin interactions with APC protein regulate epithelial tubulogenesis. of special interest J Cell Biol. 137:1997;1651-1662 Expression of amino-terminally deleted β-catenin in MDCK epithelial cells inhibits formation of cell extensions and tubule development in an in vitro tubulogenesis assay, indicating that β-catenin and β-catenin/APC interactions regulate epithelial cell migration. Cells expressing amino-terminally deleted β-catenin form aggregates that the authors note mimic the appearance of APC mutant colon polyps.
    • (1997) J Cell Biol , vol.137 , pp. 1651-1662
    • Pollack, A.L.1    Barth, A.I.M.2    Altschuler, Y.3    Nelson, W.J.4    Mostov, K.E.5
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    • -/- colon carcinoma
    • of special interest. Transfection of an APC-deficient colorectal carcinoma cell line with wild-type APC abolishes constitutively active transcription from a TCF reporter gene by competition of binding for β-catenin from β-catenin/hTCF-4 complexes to APC/β-catenin complexes.
    • -/- colon carcinoma. of special interest Science. 275:1997;1784-1787 Transfection of an APC-deficient colorectal carcinoma cell line with wild-type APC abolishes constitutively active transcription from a TCF reporter gene by competition of binding for β-catenin from β-catenin/hTCF-4 complexes to APC/β-catenin complexes.
    • (1997) Science , vol.275 , pp. 1784-1787
    • Korinek, V.1    Barker, N.2    Morin, P.J.3    Van Wichen, D.4    De Weger, R.5    Kinzler, K.6    Vogelstein, B.7    Clevers, H.8
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    • Defects in glucuronate biosynthesis disrupt Wingless signaling in Drosophila
    • of special interest
    • Haerry TE, Heslip TR, Marsh JL, O'Connor MB. Defects in glucuronate biosynthesis disrupt Wingless signaling in Drosophila. of special interest Development. 1997; This paper, as with [66,67], provides evidence that heparin sulfate proteoglycans potentiate reception of the Wingless signal.
    • (1997) Development
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    • Genetic evidence with heparin-sulfate glycosaminoglycans are involved in wingless signaling
    • of special interest. See annotation [65].
    • Binari RC, Staveley BE, Johnson WA, Godavarti R, Sasisekharan R, Manoukian AS. Genetic evidence with heparin-sulfate glycosaminoglycans are involved in wingless signaling. of special interest Development. 124:1997;2623-2632 See annotation [65].
    • (1997) Development , vol.124 , pp. 2623-2632
    • Binari, R.C.1    Staveley, B.E.2    Johnson, W.A.3    Godavarti, R.4    Sasisekharan, R.5    Manoukian, A.S.6
  • 67
    • 0342299882 scopus 로고    scopus 로고
    • The Drosophila sugarless gene modulates Wingless signaling and encodes an enzyme invoved in polysaccharide biosynthesis
    • of special interest
    • Häcker U, Lin X, Perrimon N. The Drosophila sugarless gene modulates Wingless signaling and encodes an enzyme invoved in polysaccharide biosynthesis. of special interest Development. 1997; See annotation [65].
    • (1997) Development
    • Häcker, U.1    Lin, X.2    Perrimon, N.3
  • 68
    • 0029844909 scopus 로고    scopus 로고
    • Glycosaminoglycans can modulate extracellular localization of the Wingless protein and promote signal transduction
    • of special interest. in this study, the authors demonstrate the specific binding of Wingless to heparin and that blocking appropriate glycosaminoglycan synthesis or localization inhibits Wingless signaling in cell culture. These data suggest that cell surface glycosaminoglycans promote the binding of Wingless to the cell surface, potentiating Wingless signal.
    • Reichsman F, Smith L, Cumberledge S. Glycosaminoglycans can modulate extracellular localization of the Wingless protein and promote signal transduction. of special interest J Cell Biol. 135:1996;819-827 in this study, the authors demonstrate the specific binding of Wingless to heparin and that blocking appropriate glycosaminoglycan synthesis or localization inhibits Wingless signaling in cell culture. These data suggest that cell surface glycosaminoglycans promote the binding of Wingless to the cell surface, potentiating Wingless signal.
    • (1996) J Cell Biol , vol.135 , pp. 819-827
    • Reichsman, F.1    Smith, L.2    Cumberledge, S.3


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