Regulation of Glycogen Synthase Kinase 3β and Downstream Wnt Signaling by Axin

REFERENCES

• Behrens, J., B.-A. Jerchow, M. Wurtele, J. Grimm, C. Asbrand, R. Wirtz, M. Kuhl, D. Wedlich, and J. Birchmeier 1998. Functional interaction of an axin homolog, conductin, with β-catenin, APC, and GSK-3β. Science 280:596–599.
   PubMed Web of Science ®Google Scholar
• Cadigan, K. M., and J. Nusse 1997. Wnt signaling: a common theme in animal development. Genes Dev. 11:3286–3305.
   PubMed Web of Science ®Google Scholar
• Cook, D., M. J. Fry, K. Hughes, R. Sumathipala, J. R. Woodgett, and J. Dale 1996. Wingless inactivates glycogen synthase kinase-3 via an intracellular signalling pathway which involves a protein kinase C. EMBO J. 15:4526–4536.
   PubMed Web of Science ®Google Scholar
• Dominguez, I., K. Itoh, and J. Sokol 1995. Role of glycogen synthase kinase 3 beta as a negative regulator of dorsoventral axis formation in Xenopus embryos. Proc. Natl. Acad. Sci. USA 92:8498–8502.
   PubMed Web of Science ®Google Scholar
• Emily-Fenouil, F., C. Ghiglione, G. Lhomond, T. Lepage, and J. Gache 1998. GSK-3 beta/shaggy mediates patterning along the animal-vegetal axis of the sea urchin embryo. Development 125:2489–2498.
   PubMedGoogle Scholar
• Fields, S., and J. Song 1989. A novel genetic system to detect protein-protein interactions. Nature 340:245–247.
   PubMed Web of Science ®Google Scholar
• Gluecksohn-Schoenheimer, S. 1949. The effects of a lethal mutation responsible for duplications and twinning in mouse embryos. J. Exp. Zool. 110:47–76.
   PubMedGoogle Scholar
• Goyette, M. C., K. Cho, C. L. Fasching, D. B. Levy, K. W. Kinzler, C. Paraskeva, B. Vogelstein, and J. Stanbridge 1992. Progression of colorectal cancer is associated with multiple tumor suppressor gene defects, but inhibition of tumorigenicity is accomplished by correction of any single defect via chromosome transfer. Mol. Cell. Biol. 12:1387–1395.
   PubMed Web of Science ®Google Scholar
• Greenberg, S. G., P. Davies, J. D. Schein, and J. Binder 1992. Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau. J. Biol. Chem. 267:564–569.
   PubMed Web of Science ®Google Scholar
• Harper, J. W., G. R. Adami, N. Wei, K. Keyomarski, and J. Elledge 1993. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 75:805–816.
   PubMed Web of Science ®Google Scholar
• Hart, M. J., R. Santos, I. Albert, B. Rubinfeld, and J. Polakis 1998. Downregulation of β-catenin by human axin and its association with the APC tumor suppressor, β-catenin, and GSK3B. Curr. Biol. 8:573–581.
   PubMed Web of Science ®Google Scholar
• Harwood, A. J., S. E. Plyte, J. Woodgett, H. Strutt, and J. Kay 1995. Glycogen synthase kinase 3 regulates cell fate in Dictyostelium. Cell 80:139–148.
   PubMed Web of Science ®Google Scholar
• He, X., J.-P. Saint-Jeannet, J. R. Woodgett, H. E. Varmus, and J. Dawid 1995. Glycogen synthase kinase-3 and dorsoventral patterning in Xenopus embryos. Nature 374:617–622.
   PubMedGoogle Scholar
• Heasman, J. 1997. Patterning the Xenopus blastula. Development 124:4179–4191.
   PubMedGoogle Scholar
• Hedgepeth, C., L. Conrad, Z. Zhang, H. Huang, V. Lee, and J. Klein 1997. Activation of the Wnt signaling pathway: a molecular mechanism for lithium action. Dev. Biol. 185:82–91.
   PubMed Web of Science ®Google Scholar
• Hedgepeth, C. M., M. A. Deardorff, and J. Klein 1999. Xenopus axin interacts with glycogen synthase kinase-3 beta and is expressed in the anterior midbrain. Mech. Dev. 80:147–151.
   PubMedGoogle Scholar
• Hong, M., J. Chen, P. Klein, and J. Lee 1997. Lithium reduces tau phosphorylation by direct and reversible inhibition of glycogen synthase kinase-3 in cultured human neurons. J. Biol. Chem. 272:25326–25332.
   PubMed Web of Science ®Google Scholar
• Hoshi, M., A. Takashima, K. Noguchi, M. Murayama, M. Sato, S. Kondo, Y. Saitoh, K. Ishiguro, T. Hoshino, and J. Imahori 1996. Regulation of mitochondrial pyruvate dehydrogenase activity by tau protein kinase I/glycogen synthase kinase 3B in brain. Proc. Natl. Acad. Sci. USA 93:2719–2723.
   PubMed Web of Science ®Google Scholar
• Hsu, W., L. Zeng, and J. Costantini 1999. Identification of a domain of axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain. J. Biol. Chem. 274:3439–3445.
   PubMed Web of Science ®Google Scholar
• Ikeda, S., S. Kishida, H. Yamamoto, H. Murai, S. Koyama, and J. Kikuchi 1998. Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3β and β-catenin and promotes GSK-3β-dependent phosphorylation of β-catenin. EMBO J. 17:1371–1384.
   PubMed Web of Science ®Google Scholar
• Itoh, K., V. E. Krupnik, and J. Sokol 1998. Axis determination in Xenopus involves biochemical interactions of axin, glycogen synthase kinase 3 and B-catenin. Curr. Biol. 8:591–594.
   PubMedGoogle Scholar
• Itoh, K., T. Tang, B. Neel, and J. Sokol 1995. Specific modulation of ectodermal cell fates in Xenopus embryos by glycogen synthase kinase. Dev. Suppl. 121:3979–3988.
   Google Scholar
• Jacobs-Cohen, R. J., M. Spiegelman, J. C. Cookingham, and J. Bennett 1984. Knobbly, a new dominant mutation in the mouse that affects embryonic ectoderm organization. Genet. Res. 43:43–50.
   PubMedGoogle Scholar
• Kao, K. R., Y. Masui, and J. Elinson 1986. Lithium-induced respecification of pattern in Xenopus laevis embryos. Nature 322:371–373.
   PubMed Web of Science ®Google Scholar
• Kishida, S., H. Yamamoto, S. Ikeda, M. Kishida, I. Sakamoto, S. Koyama, and J. Kikuchi 1998. Axin, a negative regulator of the Wnt signaling pathway, directly interacts with adenomatous polyposis coli and regulates the stabilization of β-catenin. J. Biol. Chem. 273:10823–10826.
   PubMed Web of Science ®Google Scholar
• Klein, P. S. Unpublished data.
   Google Scholar
• Klein, P. S., and J. Melton 1996. A molecular mechanism for the effect of lithium on development. Proc. Natl. Acad. Sci. USA 93:8455–8459.
   PubMed Web of Science ®Google Scholar
• Larabell, C. A., M. Torres, B. A. Rowning, C. Yost, J. R. Miller, M. Wu, D. Kimelman, and J. Moon 1997. 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. J. Cell Biol. 136:1123–1136.
   PubMed Web of Science ®Google Scholar
• Logan, C. Y., J. R. Miller, M. J. Ferkowicz, and J. McClay 1999. Nuclear β-catenin is required to specify vegetal cell fates in the sea urchin embryo. Development 126:345–357.
   PubMedGoogle Scholar
• Lucas, F. R., and J. Salinas 1997. WNT-7a induces axonal remodeling and increases synapsin I levels in cerebellar neurons. Dev. Biol. 192:31–44.
   PubMed Web of Science ®Google Scholar
• McCrea, P. D., W. M. Brieher, and J. Gumbiner 1993. Induction of a secondary body axis in Xenopus by antibodies to beta-catenin. J. Cell Biol. 123:477–484.
   PubMed Web of Science ®Google Scholar
• McMahon, A. P., and J. Moon 1989. Ectopic expression of the proto-oncogene int-1 in Xenopus embryos leads to duplication of the embryonic axis. Cell 58:1075–1084.
   PubMed Web of Science ®Google Scholar
• Miller, J. R., and J. Moon 1996. Signal transduction through β-catenin and specification of cell fate during embryogenesis. Genes Dev. 10:2527–2539.
   PubMed Web of Science ®Google Scholar
• Miller, J. R., and J. Moon 1996. Signal transduction through beta-catenin and specification of cell fate during embryogenesis. Genes Dev. 10:2527–2539.
   PubMed Web of Science ®Google Scholar
• Mitchell, A. P. 1994. Control of meiotic gene expression in Saccharomyces cerevisiae. Microbiol. Rev. 58:56–70.
   PubMedGoogle Scholar
• Munoz-Montano, J. R., F. J. Moreno, J. Avila, and J. Diaz-Nido 1997. Lithium inhibits Alzheimer’s disease-like tau protein phosphorylation in neurons. FEBS Lett. 411:183–188.
   PubMed Web of Science ®Google Scholar
• Otvos, L., L. Feiner, E. Lang, G. I. Szendrei, M. Goedert, and J. Lee 1994. Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404. J. Neurosci. Res. 39:669–673.
   PubMedGoogle Scholar
• Perry, W. L., T. J. Vasicek, J. J. Lee, J. M. Rossi, L. Zeng, T. Zhang, S. M. Tilghman, and J. Costantini 1995. Phenotypic and molecular analysis of a transgenic insertional allele of the mouse Fused locus. Genetics 141:321–332.
   PubMedGoogle Scholar
• Pierce, S. B., and J. Kimelman 1995. Regulation of Spemann organizer formation by the intracellular kinase Xgsk-3. Development 121:755–765.
   PubMedGoogle Scholar
• Plyte, S. E., K. Hughes, E. Nikolakaki, B. J. Pulverer, and J. Woodgett 1992. Glycogen synthase kinase-3: functions in oncogenesis and development. Biochim. Biophys. Acta 1114:147–162.
   PubMedGoogle Scholar
• Popperl, H., C. Schmidt, V. Wilson, C. R. Hume, J. Dodd, R. Krumlauf, and J. Beddington 1997. Misexpression of Cwnt8C in the mouse induces an ectopic embryonic axis and causes a truncation of the anterior neuroectoderm. Development 124:2997–3005.
   PubMed Web of Science ®Google Scholar
• Rubinfeld, B., I. Albert, E. Porfiri, C. Fiol, S. Munemitsu, and J. Polakis 1996. Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly. Science 272:1023–1026.
   PubMed Web of Science ®Google Scholar
• Rubinfeld, B., B. Souza, I. Albert, O. Muller, S. H. Chamberlain, F. R. Masiarz, S. Munemitsu, and J. Polakis 1993. Association of the APC gene product with beta-catenin. Science 262:1731–1734.
   PubMed Web of Science ®Google Scholar
• Sakanaka, C., J. B. Weiss, and J. Williams 1998. Bridging of β-catenin and glycogen synthase kinase-3β by Axin and inhibition of β-catenin-mediated transcription. Proc. Natl. Acad. Sci. USA 95:3020–3023.
   PubMed Web of Science ®Google Scholar
• Smith, L. D., W. Xu, and J. Varnold 1994. Oogenesis and oocyte isolation. Methods Cell Biol. 36:45–58.
   Google Scholar
• Stambolic, V., L. Ruel, and J. Woodgett 1996. Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells. Curr. Biol. 6:1664–1668.
   PubMed Web of Science ®Google Scholar
• Vasicek, T. J., L. Zeng, X.-J. Guan, T. Zhang, F. Constantini, and J. Tilghman 1997. Two dominant mutations in the mouse Fused gene are the result of transposon insertions. Genetics 147:777–786.
   PubMed Web of Science ®Google Scholar
• Wikramanayake, A. H., L. Huang, and J. Klein 1998. β-Catenin is essential for patterning the maternally specified animal-vegetal axis in the sea urchin embryo. Proc. Natl. Acad. Sci. USA 95:9343–9348.
   PubMedGoogle Scholar
• Woodgett, J. R. 1991. A common denominator linking glycogen metabolism, nuclear oncogenes and development. Trends Biochem. Sci. 16:177–181.
   PubMedGoogle Scholar
• Yost, C., G. H. Farr, S. B. Pierce, D. M. Ferkey, M. M. Chen, and J. Kimelman 1998. GBP, an inhibitor of GSK-3, is implicated in Xenopus development and oncogenesis. Cell 93:1031–1041.
   PubMed Web of Science ®Google Scholar
• Yost, C., M. Torres, J. Miller, E. Huang, D. Kimelman, and J. Moon 1996. The axis-inducing activity, stability, and subcellular distribution of β-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3. Genes Dev. 10:1443–1454.
   PubMed Web of Science ®Google Scholar
• Zeng, L., F. Fagotto, T. Zhang, W. Hsu, T. J. Vasicek, W. L. Perry, J. J. Lee, S. M. Tilghman, B. M. Gumbiner, and J. Costantini 1997. The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling pathway that regulates embryonic axis formation. Cell 90:181–192.
   PubMed Web of Science ®Google Scholar