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Volumn 421, Issue 6924, 2003, Pages 753-756

Cdc42 regulates GSK-3β and adenomatous polyposis coli to control cell polarity

Author keywords

[No Author keywords available]

Indexed keywords

MORPHOLOGY; PHOSPHOLIPIDS; PROTEINS; TUMORS;

EID: 0037434790     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01423     Document Type: Article
Times cited : (737)

References (28)
  • 1
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville, S. & Hall, S. Rho GTPases in cell biology. Nature 420, 629-635 (2002).
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, S.2
  • 2
    • 0035479930 scopus 로고    scopus 로고
    • Intercellular junctions and cellular polarity: The PAR-aPKC complex, a conserved core cassette playing fundamental roles in cell polarity
    • 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).
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 641-648
    • Ohno, S.1
  • 3
    • 0035799292 scopus 로고    scopus 로고
    • CDC-42 controls early cell polarity and spindle orientation in C. elegans
    • 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).
    • (2001) Curr. Biol. , vol.11 , pp. 482-488
    • Gotta, M.1    Abraham, M.C.2    Ahringer, J.3
  • 4
    • 0035799308 scopus 로고    scopus 로고
    • CDC-42 regulates PAR protein localization and function to control cellular and embryonic polarity in C. elegans
    • 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).
    • (2001) Curr. Biol. , vol.11 , pp. 474-481
    • Kay, A.J.1    Hunter, C.P.2
  • 5
    • 0035943401 scopus 로고    scopus 로고
    • Integrin-mediated Cdc42 activation controls cell polarity in migrating astrocytes through PKCζ
    • Etienne-Manneville, S. & Hall, A. Integrin-mediated Cdc42 activation controls cell polarity in migrating astrocytes through PKCζ. Cell 106, 489-498 (2001).
    • (2001) Cell , vol.106 , pp. 489-498
    • Etienne-Manneville, S.1    Hall, A.2
  • 6
    • 0029152786 scopus 로고
    • Role of glycogen synthase kinase 3β as a negative regulator of dorsoventral axis formation in Xenopus embryos
    • 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).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8498-8502
    • Dominguez, I.1    Itoh, K.2    Sokol, S.Y.3
  • 7
    • 0031595573 scopus 로고    scopus 로고
    • GSK3β/shaggy mediates patterning along the animal-vegetal axis of the sea urchin embryo
    • Emily-Fenouil, E, 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).
    • (1998) Development , vol.125 , pp. 2489-2498
    • Emily-Fenouil, E.1    Ghiglione, C.2    Lhomond, G.3    Lepage, T.4    Gache, C.5
  • 8
    • 0028931511 scopus 로고
    • Glycogen synthase kinase-3 and dorsoventral patterning in Xenopus embryos
    • 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).
    • (1995) Nature , vol.374 , pp. 617-622
    • He, X.1    Saint-Jeannet, J.-P.2    Woodgett, J.R.3    Varmus, H.E.4    Dawid, I.5
  • 9
    • 0028935672 scopus 로고
    • Regulation of Spemann organizer formation by intracellular Xgsk-3
    • Pierce, S. B. & Kimelman, D. Regulation of Spemann organizer formation by intracellular Xgsk-3. Development 121, 755-765 (1995).
    • (1995) Development , vol.121 , pp. 755-765
    • Pierce, S.B.1    Kimelman, D.2
  • 10
    • 0034665645 scopus 로고    scopus 로고
    • GSK-3: New thoughts on an old enzyme
    • Ferkey, D. M. & Kimelman, D. GSK-3: new thoughts on an old enzyme. Dev. Biol. 225, 471-479 (2000).
    • (2000) Dev. Biol. , vol.225 , pp. 471-479
    • Ferkey, D.M.1    Kimelman, D.2
  • 11
    • 0035813175 scopus 로고    scopus 로고
    • Insulin receptor substrate-2 phosphorylation is necessary for protein kinase Cζ activation by insulin in L 6hIR cells
    • 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).
    • (2001) J. Biol. Chem. , vol.276 , pp. 37109-37119
    • Oriente, F.1
  • 12
    • 0035967897 scopus 로고    scopus 로고
    • Regulation of GSK-3: A cellular multiprocessor
    • Harwood, J. A. Regulation of GSK-3: a cellular multiprocessor. Cell 105, 821-824 (2001).
    • (2001) Cell , vol.105 , pp. 821-824
    • Harwood, J.A.1
  • 13
    • 0032746701 scopus 로고    scopus 로고
    • Cell-extracellular matrix interactions stimulate the AP-1 transcription factor in an integrin-linked kinase- and glycogen synthase kinase 3-dependent manner
    • 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).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7420-7427
    • Troussard, A.A.1    Tan, C.2    Yoganathan, T.N.3    Dedhar, S.4
  • 14
    • 0033517102 scopus 로고    scopus 로고
    • Axin and Frat1 interact with Dvl and GSK, bridging Dvl to GSK in the Wnt-mediated regulation of LEF-1
    • 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).
    • (1999) EMBO J. , vol.18 , pp. 4233-4240
    • Li, L.1
  • 15
    • 0037205007 scopus 로고    scopus 로고
    • The promise and perils of Wnt signaling through β-catenin
    • Moon, R. T., Bowerman, B., Boutros, M. & Perrimon, N. The promise and perils of Wnt signaling through β-catenin. Science 296, 1644-1646 (2002).
    • (2002) Science , vol.296 , pp. 1644-1646
    • Moon, R.T.1    Bowerman, B.2    Boutros, M.3    Perrimon, N.4
  • 16
    • 0033895709 scopus 로고    scopus 로고
    • Wnt signaling and cancer
    • Polakis, P. Wnt signaling and cancer. Genes Dev. 14, 1837-1851 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 1837-1851
    • Polakis, P.1
  • 17
    • 0028987249 scopus 로고
    • Regulation of intracellular β-catenin levels by the adenomatous polyposis coli (APC) tumour-suppressor protein
    • 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).
    • (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
  • 18
    • 0029664368 scopus 로고    scopus 로고
    • Binding of GSK3β to the APC-β-catenin complex and regulation of complex assembly
    • Rubinfeld, B. et al. Binding of GSK3β to the APC-β-catenin complex and regulation of complex assembly. Science 272, 1023-1026 (1996).
    • (1996) Science , vol.272 , pp. 1023-1026
    • Rubinfeld, B.1
  • 19
    • 0036270763 scopus 로고    scopus 로고
    • The subcellular destinations of APC proteins
    • Bienz, M. The subcellular destinations of APC proteins. Nature Rev. Mol. Cell Biol. 3, 328-338 (2002).
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 328-338
    • Bienz, M.1
  • 20
    • 0037054547 scopus 로고    scopus 로고
    • 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
    • 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).
    • (2002) J. Cell Biol. , vol.157 , pp. 1041-1048
    • Mogensen, M.M.1    Tucker, J.B.2    Mackie, J.B.3    Prescott, A.R.4    Nathke, I.S.5
  • 21
    • 0029066006 scopus 로고
    • APC binds to the novel protein EB1
    • Su, L. K. et al. APC binds to the novel protein EB1. Cancer Res. 55, 2972-2977 (1995).
    • (1995) Cancer Res. , vol.55 , pp. 2972-2977
    • Su, L.K.1
  • 22
    • 0037089076 scopus 로고    scopus 로고
    • Dissecting interactions between EB1, microtubules and APC in cortical clusters at the plasma membrane
    • 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).
    • (2002) J. Cell Sci. , vol.115 , pp. 1583-1590
    • Barth, A.I.M.1    Siemers, K.A.2    Nelson, W.J.3
  • 23
    • 0029998294 scopus 로고    scopus 로고
    • Cellular phosphorylation of Tau by GSK-3β influences tau binding to microtubules and microtubule organisation
    • 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).
    • (1996) J. Cell Sci. , vol.109 , pp. 1537-1543
    • Wagner, U.1    Utton, M.2    Gallo, J.-M.3    Miller, C.C.J.4
  • 24
    • 0031800971 scopus 로고    scopus 로고
    • 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
    • Lucas, E. 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).
    • (1998) J. Cell Sci. , vol.111 , pp. 1351-1361
    • Lucas, E.R.1    Goold, R.G.2    Gordon-Weeks, P.R.3    Salinas, P.C.4
  • 25
    • 0035838422 scopus 로고    scopus 로고
    • Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization
    • 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).
    • (2001) Curr. Biol. , vol.11 , pp. 1062-1067
    • Nakamura, M.1    Zhou, X.Z.2    Lu, K.P.3
  • 26
    • 0035176077 scopus 로고    scopus 로고
    • Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3β phosphorylation
    • 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).
    • (2001) Curr. Biol. , vol.11 , pp. 44-49
    • Zumbrunn, J.1    Kinoshita, K.2    Hyman, A.A.3    Nathke, I.S.4
  • 27
    • 0035797905 scopus 로고    scopus 로고
    • Cdc42, dynein, and dynactin regulate MTOC reorientation independent of Rhoregulated microtubule stabilization
    • Palazzo, A. F. et al. Cdc42, dynein, and dynactin regulate MTOC reorientation independent of Rhoregulated microtubule stabilization. Curr. Biol. 11, 1536-1541 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1536-1541
    • Palazzo, A.F.1
  • 28
    • 0033594549 scopus 로고    scopus 로고
    • The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain
    • 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).
    • (1999) Curr. Biol. , vol.9 , pp. 425-428
    • Berrueta, L.1    Tirnauer, J.S.2    Schuyler, S.C.3    Pellman, D.4    Bierer, B.E.5


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