Cdc42 regulates GSK-3β and adenomatous polyposis coli to control cell polarity (original) (raw)

References

  1. Etienne-Manneville, S. & Hall, S. Rho GTPases in cell biology. Nature 420, 629–635 (2002)
    Article ADS CAS Google Scholar
  2. Ohno, S. Intercellular junctions and cellular polarity: the PAR–aPKC complex, a conserved core cassette playing fundamental roles in cell polarity. Curr. Opin. Cell Biol. 13, 641–648 (2001)
    Article CAS Google Scholar
  3. Gotta, M., Abraham, M. C. & Ahringer, J. CDC-42 controls early cell polarity and spindle orientation in C. elegans. Curr. Biol. 11, 482–488 (2001)
    Article CAS Google Scholar
  4. Kay, A. J. & Hunter, C. P. CDC-42 regulates PAR protein localization and function to control cellular and embryonic polarity in C. elegans. Curr. Biol. 11, 474–481 (2001)
    Article CAS Google Scholar
  5. Etienne-Manneville, S. & Hall, A. Integrin-mediated Cdc42 activation controls cell polarity in migrating astrocytes through PKCζ. Cell 106, 489–498 (2001)
    Article CAS Google Scholar
  6. Dominguez, I., Itoh, K. & Sokol, S. Y. Role of glycogen synthase kinase 3β as a negative regulator of dorsoventral axis formation in Xenopus embryos. Proc. Natl Acad. Sci. USA 92, 8498–8502 (1995)
    Article ADS CAS Google Scholar
  7. Emily-Fenouil, F., Ghiglione, C., Lhomond, G., Lepage, T. & Gache, C. GSK3β/shaggy mediates patterning along the animal-vegetal axis of the sea urchin embryo. Development 125, 2489–2498 (1998)
    CAS Google Scholar
  8. He, X., Saint-Jeannet, J.-P., Woodgett, J. R., Varmus, H. E. & Dawid, I. Glycogen synthase kinase-3 and dorsoventral patterning in Xenopus embryos. Nature 374, 617–622 (1995)
    Article ADS CAS Google Scholar
  9. Pierce, S. B. & Kimelman, D. Regulation of Spemann organizer formation by intracellular Xgsk-3. Development 121, 755–765 (1995)
    CAS Google Scholar
  10. Ferkey, D. M. & Kimelman, D. GSK-3: new thoughts on an old enzyme. Dev. Biol. 225, 471–479 (2000)
    Article CAS Google Scholar
  11. Oriente, F. et al. Insulin receptor substrate-2 phosphorylation is necessary for protein kinase Cζ activation by insulin in L6hIR cells. J. Biol. Chem. 276, 37109–37119 (2001)
    Article CAS Google Scholar
  12. Harwood, J. A. Regulation of GSK-3: a cellular multiprocessor. Cell 105, 821–824 (2001)
    Article CAS Google Scholar
  13. Troussard, A. A., Tan, C., Yoganathan, T. N. & Dedhar, S. Cell–extracellular matrix interactions stimulate the AP-1 transcription factor in an integrin-linked kinase- and glycogen synthase kinase 3-dependent manner. Mol. Cell. Biol. 19, 7420–7427 (1999)
    Article CAS Google Scholar
  14. Li, L. et al. Axin and Frat1 interact with Dvl and GSK, bridging Dvl to GSK in the Wnt-mediated regulation of LEF-1. EMBO J. 18, 4233–4240 (1999)
    Article CAS Google Scholar
  15. Moon, R. T., Bowerman, B., Boutros, M. & Perrimon, N. The promise and perils of Wnt signaling through β-catenin. Science 296, 1644–1646 (2002)
    Article ADS CAS Google Scholar
  16. Polakis, P. Wnt signaling and cancer. Genes Dev. 14, 1837–1851 (2000)
    CAS Google Scholar
  17. Munemitsu, S., Albert, I., Souza, B., Rubinfeld, B. & Polakis, P. Regulation of intracellular β-catenin levels by the adenomatous polyposis coli (APC) tumour-suppressor protein. Proc. Natl Acad. Sci. USA 92, 3046–3050 (1995)
    Article ADS CAS Google Scholar
  18. Rubinfeld, B. et al. Binding of GSK3β to the APC-β-catenin complex and regulation of complex assembly. Science 272, 1023–1026 (1996)
    Article ADS CAS Google Scholar
  19. Bienz, M. The subcellular destinations of APC proteins. Nature Rev. Mol. Cell Biol. 3, 328–338 (2002)
    Article CAS Google Scholar
  20. Mogensen, M. M., Tucker, J. B., Mackie, J. B., Prescott, A. R. & Nathke, I. S. The adenomatous polyposis coli protein unambiguously localizes to microtubule plus ends and is involved in establishing parrallel arrays of microtubule bundles in highly polarized epithelial cells. J. Cell Biol. 157, 1041–1048 (2002)
    Article CAS Google Scholar
  21. Su, L. K. et al. APC binds to the novel protein EB1. Cancer Res. 55, 2972–2977 (1995)
    CAS Google Scholar
  22. Barth, A. I. M., Siemers, K. A. & Nelson, W. J. Dissecting interactions between EB1, microtubules and APC in cortical clusters at the plasma membrane. J. Cell Sci. 115, 1583–1590 (2002)
    CAS PubMed Central Google Scholar
  23. Wagner, U., Utton, M., Gallo, J.-M. & Miller, C. C. J. Cellular phosphorylation of Tau by GSK-3β influences tau binding to microtubules and microtubule organisation. J. Cell Sci. 109, 1537–1543 (1996)
    CAS Google Scholar
  24. Lucas, F. R., Goold, R. G., Gordon-Weeks, P. R. & Salinas, P. C. Inhibition of GSK-3β leading to the loss of phosphorylated MAP-1B is an early event in axonal remodelling induced by WNT-7a or lithium. J. Cell Sci. 111, 1351–1361 (1998)
    CAS Google Scholar
  25. Nakamura, M., Zhou, X. Z. & Lu, K. P. Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization. Curr. Biol. 11, 1062–1067 (2001)
    Article CAS Google Scholar
  26. Zumbrunn, J., Kinoshita, K., Hyman, A. A. & Nathke, I. S. Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3β phosphorylation. Curr. Biol. 11, 44–49 (2001)
    Article CAS Google Scholar
  27. Palazzo, A. F. et al. Cdc42, dynein, and dynactin regulate MTOC reorientation independent of Rho-regulated microtubule stabilization. Curr. Biol. 11, 1536–1541 (2001)
    Article CAS Google Scholar
  28. Berrueta, L., Tirnauer, J. S., Schuyler, S. C., Pellman, D. & Bierer, B. E. The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain. Curr. Biol. 9, 425–428 (1999)
    Article CAS Google Scholar

Download references