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Volumn 455, Issue 7217, 2008, Pages 1205-1209

Glycogen synthase kinase 3 in MLL leukaemia maintenance and targeted therapy

Author keywords

[No Author keywords available]

Indexed keywords

2 (2,4 DICHLOROPHENYL) 3 (1 METHYL 3 INDOLYL)MALEIMIDE; GLYCOGEN SYNTHASE KINASE 3; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; MIXED LINEAGE LEUKEMIA PROTEIN; PROTEIN SERINE THREONINE KINASE;

EID: 55249120170     PISSN: 00280836     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/nature07284     Document Type: Article
Times cited : (243)

References (43)
  • 1
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • Doble, B. W. & Woodgett, J. R. GSK-3: tricks of the trade for a multi-tasking kinase. J. Cell Sci. 116, 1175-1186 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 2
    • 33750893159 scopus 로고    scopus 로고
    • GSK3 at the edge: Regulation of developmental specification and cell polarization
    • Kim, L. & Kimmel, A. R. GSK3 at the edge: regulation of developmental specification and cell polarization. Curr. Drug Targets 7, 1411-1419 (2006).
    • (2006) Curr. Drug Targets , vol.7 , pp. 1411-1419
    • Kim, L.1    Kimmel, A.R.2
  • 4
    • 0023656594 scopus 로고
    • Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3
    • Fiol, C. J., Mahrenholz, A. M., Wang, Y., Roeske, R. W. & Roach, P. J. Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3. J. Biol. Chem. 262, 14042-14048 (1987).
    • (1987) J. Biol. Chem , vol.262 , pp. 14042-14048
    • Fiol, C.J.1    Mahrenholz, A.M.2    Wang, Y.3    Roeske, R.W.4    Roach, P.J.5
  • 5
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross, D. A., Alessi, D. R., Cohen, P., Andjelkovich, M. & Hemmings, B. A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378, 785-789 (1995).
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 6
    • 0036398986 scopus 로고    scopus 로고
    • The role of glycogen synthase kinase-3 in insulin resistance and type 2 diabetes
    • Kaidanovich, O. & Eldar-Finkelman, H. The role of glycogen synthase kinase-3 in insulin resistance and type 2 diabetes. Expert Opin. Ther. Targets 6, 555-561 (2002).
    • (2002) Expert Opin. Ther. Targets , vol.6 , pp. 555-561
    • Kaidanovich, O.1    Eldar-Finkelman, H.2
  • 7
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation
    • Hoeflich, K. P. et al. Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation. Nature 406, 86-90 (2000).
    • (2000) Nature , vol.406 , pp. 86-90
    • Hoeflich, K.P.1
  • 8
    • 23944486750 scopus 로고    scopus 로고
    • Toll-like receptor-mediated cytokine production is differentially regulated by glycogen synthase kinase 3
    • Martin, M., Rehani, K., Jope, R. S. & Michalek, S. M. Toll-like receptor-mediated cytokine production is differentially regulated by glycogen synthase kinase 3. Nature Immunol. 6, 777-784 (2005).
    • (2005) Nature Immunol , vol.6 , pp. 777-784
    • Martin, M.1    Rehani, K.2    Jope, R.S.3    Michalek, S.M.4
  • 9
    • 0033850796 scopus 로고    scopus 로고
    • Wnt signaling function in Alzheimer's disease
    • De Ferrari, G. V. & Inestrosa, N. C. Wnt signaling function in Alzheimer's disease. Brain Res. Rev. 33, 1-12 (2000).
    • (2000) Brain Res. Rev , vol.33 , pp. 1-12
    • De Ferrari, G.V.1    Inestrosa, N.C.2
  • 10
    • 0029964851 scopus 로고    scopus 로고
    • Signal transduction through β-catenin and specification of cell fate during embryogenesis
    • Miller, J. R. & Moon, R. T. Signal transduction through β-catenin and specification of cell fate during embryogenesis. Genes Dev. 10, 2527-2539 (1996).
    • (1996) Genes Dev , vol.10 , pp. 2527-2539
    • Miller, J.R.1    Moon, R.T.2
  • 11
    • 0037041470 scopus 로고    scopus 로고
    • Shaggy/GSK3 antagonizes Hedgehog signalling by regulating Cubitus interruptus
    • Jia, J. et al. Shaggy/GSK3 antagonizes Hedgehog signalling by regulating Cubitus interruptus. Nature 416, 548-552 (2002).
    • (2002) Nature , vol.416 , pp. 548-552
    • Jia, J.1
  • 12
    • 0036153448 scopus 로고    scopus 로고
    • The Wnts
    • Miller, J. R. The Wnts. Genome Biol 3, 3001 (2002).
    • (2002) Genome Biol , vol.3 , pp. 3001
    • Miller, J.R.1
  • 13
    • 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. et al. 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 (1996).
    • (1996) Genes Dev , vol.10 , pp. 1443-1454
    • Yost, C.1
  • 15
    • 0034306997 scopus 로고    scopus 로고
    • Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability
    • Sears, R. et al. Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability. Genes Dev. 14, 2501-2514 (2000).
    • (2000) Genes Dev , vol.14 , pp. 2501-2514
    • Sears, R.1
  • 16
    • 0027512538 scopus 로고
    • Glycogen synthase kinase 3 phosphorylates Jun family members in vitro and negatively regulates their transactivating potential in intact cells
    • Nikolakaki, E., Coffer, P. J., Hemelsoet, R., Woodgett, J. R. & Defize, L. H. Glycogen synthase kinase 3 phosphorylates Jun family members in vitro and negatively regulates their transactivating potential in intact cells. Oncogene 8, 833-840 (1993).
    • (1993) Oncogene , vol.8 , pp. 833-840
    • Nikolakaki, E.1    Coffer, P.J.2    Hemelsoet, R.3    Woodgett, J.R.4    Defize, L.H.5
  • 17
    • 30044444251 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 is an in vivo regulator of hematopoietic stem cell repopulation
    • Trowbridge, J. J., Xenocostas, A., Moon, R. T. & Bhatia, M. Glycogen synthase kinase-3 is an in vivo regulator of hematopoietic stem cell repopulation. Nature Med. 12, 89-98 (2006).
    • (2006) Nature Med , vol.12 , pp. 89-98
    • Trowbridge, J.J.1    Xenocostas, A.2    Moon, R.T.3    Bhatia, M.4
  • 18
    • 1242267927 scopus 로고    scopus 로고
    • Maintenance of pluripotency in human and mouse embryonic stem cells through activation of Wnt signaling by a pharmacological GSK-3-specific inhibitor
    • Sato, N., Meijer, L., Skaltsounis, L., Greengard, P. & Brivanlou, A. H. Maintenance of pluripotency in human and mouse embryonic stem cells through activation of Wnt signaling by a pharmacological GSK-3-specific inhibitor. Nature Med. 10, 55-63 (2004).
    • (2004) Nature Med , vol.10 , pp. 55-63
    • Sato, N.1    Meijer, L.2    Skaltsounis, L.3    Greengard, P.4    Brivanlou, A.H.5
  • 19
    • 0035839952 scopus 로고    scopus 로고
    • Molecular mechanisms of leukemogenesis mediated by MLL fusion proteins
    • Ayton, P. M. & Cleary, M. L. Molecular mechanisms of leukemogenesis mediated by MLL fusion proteins. Oncogene 20, 5695-5707 (2001).
    • (2001) Oncogene , vol.20 , pp. 5695-5707
    • Ayton, P.M.1    Cleary, M.L.2
  • 20
    • 4644220954 scopus 로고    scopus 로고
    • MLL: A histone methyltransferase disrupted in leukemia
    • Hess, J. L. MLL: a histone methyltransferase disrupted in leukemia. Trends Mol. Med. 10, 500-507 (2004).
    • (2004) Trends Mol. Med , vol.10 , pp. 500-507
    • Hess, J.L.1
  • 21
    • 0030791974 scopus 로고    scopus 로고
    • Immortalization and leukemic transformation of a myelomonocytic precursor by retrovirally transduced HRXENL
    • Lavau, C., Szilvassy, S. J., Slany, R. & Cleary, M. L. Immortalization and leukemic transformation of a myelomonocytic precursor by retrovirally transduced HRXENL. EMBO J. 16, 4226-4237 (1997).
    • (1997) EMBO J , vol.16 , pp. 4226-4237
    • Lavau, C.1    Szilvassy, S.J.2    Slany, R.3    Cleary, M.L.4
  • 22
    • 33749440584 scopus 로고    scopus 로고
    • Identification and characterization of leukemia stem cells in murine MLL-AF9 acute myeloid leukemia
    • Somervaille, T. C. & Cleary, M. L. Identification and characterization of leukemia stem cells in murine MLL-AF9 acute myeloid leukemia. Cancer Cell 10, 257-268 (2006).
    • (2006) Cancer Cell , vol.10 , pp. 257-268
    • Somervaille, T.C.1    Cleary, M.L.2
  • 23
    • 34249675397 scopus 로고    scopus 로고
    • Lithium therapy improves neurological function and hippocampal dendritic arborization in a spinocerebellar ataxia type 1 mouse model
    • Watase, K. et al. Lithium therapy improves neurological function and hippocampal dendritic arborization in a spinocerebellar ataxia type 1 mouse model. PLoS Med. 4, e182 (2007).
    • (2007) PLoS Med , vol.4
    • Watase, K.1
  • 24
    • 0033054464 scopus 로고    scopus 로고
    • The oncogenic activation of beta-catenin
    • Polakis, P. The oncogenic activation of beta-catenin. Curr. Opin. Genet. Dev. 9, 15-21 (1999).
    • (1999) Curr. Opin. Genet. Dev , vol.9 , pp. 15-21
    • Polakis, P.1
  • 25
    • 27844432603 scopus 로고    scopus 로고
    • AKT signaling in normal and malignant cells
    • Testa, J. R. & Tsichlis, P. N. AKT signaling in normal and malignant cells. Oncogene 24, 7391-7393 (2005).
    • (2005) Oncogene , vol.24 , pp. 7391-7393
    • Testa, J.R.1    Tsichlis, P.N.2
  • 27
    • 20044380143 scopus 로고    scopus 로고
    • Menin and MLL cooperatively regulate expression of cyclin-dependent kinase inhibitors
    • Milne, T. A. et al. Menin and MLL cooperatively regulate expression of cyclin-dependent kinase inhibitors. Proc. Natl Acad. Sci. USA 102, 749-754 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 749-754
    • Milne, T.A.1
  • 28
    • 26844555530 scopus 로고    scopus 로고
    • The menin tumor suppressor protein is an essential oncogenic cofactor for MLL-associated leukemogenesis
    • Yokoyama, A. et al. The menin tumor suppressor protein is an essential oncogenic cofactor for MLL-associated leukemogenesis. Cell 123, 207-218 (2005).
    • (2005) Cell , vol.123 , pp. 207-218
    • Yokoyama, A.1
  • 29
    • 10744224167 scopus 로고    scopus 로고
    • Menin associates with a trithorax family histone methyltransferase complex and with the Hoxc8 locus
    • Hughes, C. M. et al. Menin associates with a trithorax family histone methyltransferase complex and with the Hoxc8 locus. Mol. Cell 13, 587-597 (2004).
    • (2004) Mol. Cell , vol.13 , pp. 587-597
    • Hughes, C.M.1
  • 32
    • 0036031664 scopus 로고    scopus 로고
    • G.-Amlak, M. et al. Regulation of myeloma cell growth through Akt/Gsk3/forkhead signaling pathway. Biochem. Biophys. Res. Commun. 297, 760-764 (2002).
    • G.-Amlak, M. et al. Regulation of myeloma cell growth through Akt/Gsk3/forkhead signaling pathway. Biochem. Biophys. Res. Commun. 297, 760-764 (2002).
  • 33
    • 0032831130 scopus 로고    scopus 로고
    • Mll rearrangements in haematological malignancies: Lessons from clinical and biological studies
    • Dimartino, J. F. & Cleary, M. L. Mll rearrangements in haematological malignancies: lessons from clinical and biological studies. Br. J. Haematol. 106, 614-626 (1999).
    • (1999) Br. J. Haematol , vol.106 , pp. 614-626
    • Dimartino, J.F.1    Cleary, M.L.2
  • 34
    • 0027172909 scopus 로고
    • Molecular rearrangements on chromosome 11q23 predominate in infant acute lymphoblastic leukemia and are associated with specific biologic variables and poor outcome
    • Chen, C. S. et al. Molecular rearrangements on chromosome 11q23 predominate in infant acute lymphoblastic leukemia and are associated with specific biologic variables and poor outcome. Blood 81, 2386-2393 (1993).
    • (1993) Blood , vol.81 , pp. 2386-2393
    • Chen, C.S.1
  • 35
    • 0036788036 scopus 로고    scopus 로고
    • The Wnt signaling pathway in bipolar disorder
    • Gould, T. D. & Manji, H. K. The Wnt signaling pathway in bipolar disorder. Neuroscientist 8, 497-511 (2002).
    • (2002) Neuroscientist , vol.8 , pp. 497-511
    • Gould, T.D.1    Manji, H.K.2
  • 36
    • 33646376411 scopus 로고    scopus 로고
    • Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells
    • Yilmaz, O. H. et al. Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells. Nature 441, 475-482 (2006).
    • (2006) Nature , vol.441 , pp. 475-482
    • Yilmaz, O.H.1
  • 37
    • 0036837682 scopus 로고    scopus 로고
    • Transformation of bone marrow B-cell progenitors by E2A-HlF requires coexpression of BCL-2
    • Smith, K. S., Rhee, J. W. & Cleary, M. L. Transformation of bone marrow B-cell progenitors by E2A-HlF requires coexpression of BCL-2. Mol. Cell. Biol. 22, 7678-7687 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 7678-7687
    • Smith, K.S.1    Rhee, J.W.2    Cleary, M.L.3
  • 38
    • 0042872887 scopus 로고    scopus 로고
    • MLL-GAS7 transforms multipotent hematopoietic progenitors and induces mixed lineage leukemias in mice
    • So, C. W. et al. MLL-GAS7 transforms multipotent hematopoietic progenitors and induces mixed lineage leukemias in mice. Cancer Cell 3, 161-171 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 161-171
    • So, C.W.1
  • 39
    • 0030849122 scopus 로고    scopus 로고
    • Chimeric oncoprotein E2a-Pbx1 induces apoptosis of hematopoietic cells by a p53-independent mechanism that is suppressed by Bcl-2
    • Smith, K. S., Jacobs, Y., Chang, C. P.&Cleary, M. L. Chimeric oncoprotein E2a-Pbx1 induces apoptosis of hematopoietic cells by a p53-independent mechanism that is suppressed by Bcl-2. Oncogene 14, 2917-2926 (1997).
    • (1997) Oncogene , vol.14 , pp. 2917-2926
    • Smith, K.S.1    Jacobs, Y.2    Chang, C.P.3    Cleary, M.L.4
  • 40
    • 0032927877 scopus 로고    scopus 로고
    • CREB binding protein interacts with nucleoporin-specific FG repeats that activate transcription and mediate NUP98-HOXA9 oncogenicity
    • Kasper, L. H. et al. CREB binding protein interacts with nucleoporin-specific FG repeats that activate transcription and mediate NUP98-HOXA9 oncogenicity. Mol. Cell. Biol. 19, 764-776 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , pp. 764-776
    • Kasper, L.H.1
  • 41
    • 0032496239 scopus 로고    scopus 로고
    • Construction and characterization of a conditionally active version of the serine/threonine kinase Akt
    • Kohn, A. D. et al. Construction and characterization of a conditionally active version of the serine/threonine kinase Akt. J. Biol. Chem. 273, 11937-11943 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 11937-11943
    • Kohn, A.D.1
  • 42
    • 0036723650 scopus 로고    scopus 로고
    • MLL-AFX requires the transcriptional effector domains of AFX to transform myeloid progenitors and transdominantly interfere with forkhead protein function
    • So, C. W. & Cleary, M. L. MLL-AFX requires the transcriptional effector domains of AFX to transform myeloid progenitors and transdominantly interfere with forkhead protein function. Mol. Cell. Biol. 22, 6542-6552 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 6542-6552
    • So, C.W.1    Cleary, M.L.2
  • 43
    • 3142708570 scopus 로고    scopus 로고
    • Cre-lox-regulated conditional RNA interference from transgenes
    • Ventura, A. et al. Cre-lox-regulated conditional RNA interference from transgenes. Proc. Natl Acad. Sci. USA 101, 10380-10385 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10380-10385
    • Ventura, A.1


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