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Volumn 457, Issue 1, 2014, Pages 43-56

A novel DYRK1B inhibitor AZ191 demonstrates that DYRK1B acts independently of GSK3Β to phosphorylate cyclin D1 at Thr286, not Thr 288

Author keywords

AZ191; Cell cycle; Cyclin D1; Dual specificity tyrosine phosphorylation regulated kinase 1B (DYRK1B); Glycogen synthase kinase 3 (GSK3 )

Indexed keywords

AZ 191; AZ 4216; CYCLIN D1; DUAL SPECIFICITY TYROSINE PHOSPHORYLATION REGULATED KINASE 1B; GLYCOGEN SYNTHASE KINASE 3BETA; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; THREONINE; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84890011858     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20130461     Document Type: Article
Times cited : (61)

References (45)
  • 1
    • 0032603540 scopus 로고    scopus 로고
    • Structural and functional characteristics of Dyrk, a novel subfamily of protein kinases with dual specificity
    • Becker, W. and Joost, H. G. (1999) Structural and functional characteristics of Dyrk, a novel subfamily of protein kinases with dual specificity. Prog. Nucleic Acid Res. Mol. Biol. 62, 1-17
    • (1999) Prog. Nucleic Acid Res. Mol. Biol. , vol.62 , pp. 1-17
    • Becker, W.1    Joost, H.G.2
  • 3
    • 20444387985 scopus 로고    scopus 로고
    • Activation-loop autophosphorylation is mediated by a novel transitional intermediate form of DYRKs
    • Lochhead, P. A., Sibbet, G., Morrice, N. and Cleghon, V. (2005) Activation-loop autophosphorylation is mediated by a novel transitional intermediate form of DYRKs. Cell 121, 925-36
    • (2005) Cell , vol.121 , pp. 925-936
    • Lochhead, P.A.1    Sibbet, G.2    Morrice, N.3    Cleghon, V.4
  • 4
    • 0032475973 scopus 로고    scopus 로고
    • Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases
    • Becker, W., Weber, Y., Wetzel, K., Eirmbter, K., Tejedor, F. J. and Joost, H. G. (1998) Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases. J. Biol. Chem. 273, 25893-25902
    • (1998) J. Biol. Chem. , vol.273 , pp. 25893-25902
    • Becker, W.1    Weber, Y.2    Wetzel, K.3    Eirmbter, K.4    Tejedor, F.J.5    Joost, H.G.6
  • 5
    • 0142071703 scopus 로고    scopus 로고
    • Mirk/dyrk1B is a Rho-induced kinase active in skeletal muscle differentiation
    • Deng, X., Ewton, D. Z., Pawlikowski, B., Maimone, M. and Friedman, E. (2003) Mirk/dyrk1B is a Rho-induced kinase active in skeletal muscle differentiation. J. Biol. Chem. 278, 41347-41354
    • (2003) J. Biol. Chem. , vol.278 , pp. 41347-41354
    • Deng, X.1    Ewton, D.Z.2    Pawlikowski, B.3    Maimone, M.4    Friedman, E.5
  • 9
    • 70349947061 scopus 로고    scopus 로고
    • Harmine specifically inhibits protein kinase DYRK1A and interferes with neurite formation
    • Gockler, N., Jofre, G., Papadopoulos, C., Soppa, U., Tejedor, F. J. and Becker, W. (2009) Harmine specifically inhibits protein kinase DYRK1A and interferes with neurite formation. FEBS J. 276, 6324-6337
    • (2009) FEBS J , vol.276 , pp. 6324-6337
    • Gockler, N.1    Jofre, G.2    Papadopoulos, C.3    Soppa, U.4    Tejedor, F.J.5    Becker, W.6
  • 11
    • 0028970609 scopus 로고
    • Transforming p21ras mutants and c-Ets-2 activate the cyclin D1 promoter through distinguishable regions
    • Albanese, C., Johnson, J., Watanabe, G., Eklund, N., Vu, D., Arnold, A. and Pestell, R. G. (1995) Transforming p21ras mutants and c-Ets-2 activate the cyclin D1 promoter through distinguishable regions. J. Biol. Chem. 270, 23589-23597
    • (1995) J. Biol. Chem. , vol.270 , pp. 23589-23597
    • Albanese, C.1    Johnson, J.2    Watanabe, G.3    Eklund, N.4    Vu, D.5    Arnold, A.6    Pestell, R.G.7
  • 13
    • 0013439945 scopus 로고    scopus 로고
    • Cycling to cancer with cyclin D1
    • Diehl, J. A. (2002) Cycling to cancer with cyclin D1. Cancer Biol. Ther. 1, 226-231
    • (2002) Cancer Biol. Ther. , vol.1 , pp. 226-231
    • Diehl, J.A.1
  • 14
    • 0033080511 scopus 로고    scopus 로고
    • Cyclin D1 inhibits cell proliferation through binding to PCNA and cdk2
    • Fukami-Kobayashi, J. and Mitsui, Y. (1999) Cyclin D1 inhibits cell proliferation through binding to PCNA and cdk2. Exp. Cell Res. 246, 338-347
    • (1999) Exp. Cell Res. , vol.246 , pp. 338-347
    • Fukami-Kobayashi, J.1    Mitsui, Y.2
  • 15
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization
    • Diehl, J. A., Cheng, M., Roussel, M. F. and Sherr, C. J. (1998) Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization. Genes Dev. 12, 3499-3511
    • (1998) Genes Dev , vol.12 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 16
    • 0030916209 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway
    • Diehl, J. A., Zindy, F. and Sherr, C. J. (1997) Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway. Genes Dev. 11, 957-972
    • (1997) Genes Dev , vol.11 , pp. 957-972
    • Diehl, J.A.1    Zindy, F.2    Sherr, C.J.3
  • 17
    • 0034671768 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation
    • Alt, J. R., Cleveland, J. L., Hannink, M. and Diehl, J. A. (2000) Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation. Genes Dev. 14, 3102-3114
    • (2000) Genes Dev , vol.14 , pp. 3102-3114
    • Alt, J.R.1    Cleveland, J.L.2    Hannink, M.3    Diehl, J.A.4
  • 18
    • 33644836891 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor, trichostatin A induces ubiquitin-dependent cyclin D1 degradation in MCF-7 breast cancer cells
    • Alao, J. P., Stavropoulou, A. V., Lam, E. W., Coombes, R. C. and Vigushin, D. M. (2006) Histone deacetylase inhibitor, trichostatin A induces ubiquitin-dependent cyclin D1 degradation in MCF-7 breast cancer cells. Mol. Cancer 5, 8
    • (2006) Mol. Cancer , vol.5 , pp. 8
    • Alao, J.P.1    Stavropoulou, A.V.2    Lam, E.W.3    Coombes, R.C.4    Vigushin, D.M.5
  • 20
    • 0037211485 scopus 로고    scopus 로고
    • Rapid turnover of cell-cycle regulators found in Mirk/dyrk1B transfectants
    • Ewton, D. Z., Lee, K., Deng, X., Lim, S. and Friedman, E. (2003) Rapid turnover of cell-cycle regulators found in Mirk/dyrk1B transfectants. Int. J. Cancer 103, 21-28
    • (2003) Int. J. Cancer , vol.103 , pp. 21-28
    • Ewton, D.Z.1    Lee, K.2    Deng, X.3    Lim, S.4    Friedman, E.5
  • 21
    • 3042684281 scopus 로고    scopus 로고
    • Mirk/dyrk1B kinase destabilizes cyclin D1 by phosphorylation at threonine 288
    • Zou, Y., Ewton, D. Z., Deng, X., Mercer, S. E. and Friedman, E. (2004) Mirk/dyrk1B kinase destabilizes cyclin D1 by phosphorylation at threonine 288. J. Biol. Chem. 279, 27790-27798
    • (2004) J. Biol. Chem. , vol.279 , pp. 27790-27798
    • Zou, Y.1    Ewton, D.Z.2    Deng, X.3    Mercer, S.E.4    Friedman, E.5
  • 22
    • 52149124127 scopus 로고    scopus 로고
    • ERK1/2 and p38 cooperate to delay progression through G1 by promoting cyclin D1 protein turnover
    • Densham, R. M., Todd, D. E., Balmanno, K. and Cook, S. J. (2008) ERK1/2 and p38 cooperate to delay progression through G1 by promoting cyclin D1 protein turnover. Cell. Signalling 20, 1986-1994
    • (2008) Cell. Signalling , vol.20 , pp. 1986-1994
    • Densham, R.M.1    Todd, D.E.2    Balmanno, K.3    Cook, S.J.4
  • 24
    • 1542275411 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases 1/2 are serum-stimulated "Bim(EL) kinases" that bind to the BH3-only protein Bim(EL) causing its phosphorylation and turnover
    • Ley, R., Ewings, K. E., Hadfield, K., Howes, E., Balmanno, K. and Cook, S. J. (2004) Extracellular signal-regulated kinases 1/2 are serum-stimulated "Bim(EL) kinases" that bind to the BH3-only protein Bim(EL) causing its phosphorylation and turnover. J. Biol. Chem. 279, 8837-8847
    • (2004) J. Biol. Chem. , vol.279 , pp. 8837-8847
    • Ley, R.1    Ewings, K.E.2    Hadfield, K.3    Howes, E.4    Balmanno, K.5    Cook, S.J.6
  • 27
    • 0034723403 scopus 로고    scopus 로고
    • Specificity determinants of substrate recognition by the protein kinase DYRK1A
    • Himpel, S., Tegge, W., Frank, R., Leder, S., Joost, H. G. and Becker, W. (2000) Specificity determinants of substrate recognition by the protein kinase DYRK1A. J. Biol. Chem. 275, 2431-2438
    • (2000) J. Biol. Chem. , vol.275 , pp. 2431-2438
    • Himpel, S.1    Tegge, W.2    Frank, R.3    Leder, S.4    Joost, H.G.5    Becker, W.6
  • 30
    • 0037339766 scopus 로고    scopus 로고
    • Selective glycogen synthase kinase 3 inhibitors potentiate insulin activation of glucose transport and utilization in vitro and in vivo
    • Ring, D. B., Johnson, K. W., Henriksen, E. J., Nuss, J. M., Goff, D., Kinnick, T. R., Ma, S. T., Reeder, J. W., Samuels, I., Slabiak, T. et al. (2003) Selective glycogen synthase kinase 3 inhibitors potentiate insulin activation of glucose transport and utilization in vitro and in vivo. Diabetes 52, 588-595
    • (2003) Diabetes , vol.52 , pp. 588-595
    • Ring, D.B.1    Johnson, K.W.2    Henriksen, E.J.3    Nuss, J.M.4    Goff, D.5    Kinnick, T.R.6    Ma, S.T.7    Reeder, J.W.8    Samuels, I.9    Slabiak, T.10
  • 31
    • 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., Torres, M., Miller, J. R., Huang, E., Kimelman, D. and Moon, R. T. (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
    • (1996) Genes Dev , vol.10 , pp. 1443-1454
    • Yost, C.1    Torres, M.2    Miller, J.R.3    Huang, E.4    Kimelman, D.5    Moon, R.T.6
  • 32
    • 0027154638 scopus 로고
    • Cyclin D1 is a nuclear protein required for cell cycle progression in G1
    • Baldin, V., Lukas, J., Marcote, M. J., Pagano, M. and Draetta, G. (1993) Cyclin D1 is a nuclear protein required for cell cycle progression in G1. Genes Dev. 7, 812-821
    • (1993) Genes Dev , vol.7 , pp. 812-821
    • Baldin, V.1    Lukas, J.2    Marcote, M.J.3    Pagano, M.4    Draetta, G.5
  • 33
    • 2542489078 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor p27Kip1 is stabilized in G0 by Mirk/dyrk1B kinase
    • Deng, X., Mercer, S. E., Shah, S., Ewton, D. Z. and Friedman, E. (2004) The cyclin-dependent kinase inhibitor p27Kip1 is stabilized in G0 by Mirk/dyrk1B kinase. J. Biol. Chem. 279, 22498-22504
    • (2004) J. Biol. Chem. , vol.279 , pp. 22498-22504
    • Deng, X.1    Mercer, S.E.2    Shah, S.3    Ewton, D.Z.4    Friedman, E.5
  • 34
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • Harper, J. W., Adami, G. R., Wei, N., Keyomarsi, K. and Elledge, S. J. (1993) The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 75, 805-816
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 35
    • 21844468764 scopus 로고    scopus 로고
    • Mirk/Dyrk1B mediates survival during the differentiation of C2C12 myoblasts
    • Mercer, S. E., Ewton, D. Z., Deng, X., Deng, S., Deng, T. R. and Deng, E. (2005) Mirk/Dyrk1B mediates survival during the differentiation of C2C12 myoblasts. J. Biol. Chem. 280, 25788-25801
    • (2005) J. Biol. Chem. , vol.280 , pp. 25788-25801
    • Mercer, S.E.1    Ewton, D.Z.2    Deng, X.3    Deng, S.4    Deng, T.R.5    Deng, E.6
  • 36
    • 0028176483 scopus 로고
    • Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals
    • Polyak, K., Lee, M. H., Erdjument-Bromage, H., Koff, A., Roberts, J. M., Tempst, P. and Massague, J. (1994) Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals. Cell 78, 59-66
    • (1994) Cell , vol.78 , pp. 59-66
    • Polyak, K.1    Lee, M.H.2    Erdjument-Bromage, H.3    Koff, A.4    Roberts, J.M.5    Tempst, P.6    Massague, J.7
  • 38
    • 84874936048 scopus 로고    scopus 로고
    • Ovarian cancer cells, not normal cells, are damaged by Mirk/Dyrk1B kinase inhibition
    • Hu, J., Deng, H. and Friedman, E. A. (2013) Ovarian cancer cells, not normal cells, are damaged by Mirk/Dyrk1B kinase inhibition. Int. J. Cancer 132, 2258-2269
    • (2013) Int. J. Cancer , vol.132 , pp. 2258-2269
    • Hu, J.1    Deng, H.2    Friedman, E.A.3
  • 39
    • 33845985316 scopus 로고    scopus 로고
    • Involvement of GSK-3β and DYRK1B in differentiation-inducing factor-3-induced phosphorylation of cyclin D1 in HeLa cells
    • Takahashi-Yanaga, F., Mori, J., Matsuzaki, E., Watanabe, Y., Hirata, M., Miwa, Y., Morimoto, S. and Sasaguri, T. (2006) Involvement of GSK-3β and DYRK1B in differentiation-inducing factor-3-induced phosphorylation of cyclin D1 in HeLa cells. J. Biol. Chem. 281, 38489-38497
    • (2006) J. Biol. Chem. , vol.281 , pp. 38489-38497
    • Takahashi-Yanaga, F.1    Mori, J.2    Matsuzaki, E.3    Watanabe, Y.4    Hirata, M.5    Miwa, Y.6    Morimoto, S.7    Sasaguri, T.8
  • 40
    • 0035340295 scopus 로고    scopus 로고
    • The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bε at Ser539 and the microtubule-associated protein tau at Thr212: Potential role for DYRK as a glycogen synthase kinase 3-priming kinase
    • Woods, Y. L., Cohen, P., Becker, W., Jakes, R., Goedert, M., Wang, X. and Proud, C. G. (2001) The kinase DYRK phosphorylates protein-synthesis initiation factor eIF2Bε at Ser539 and the microtubule-associated protein tau at Thr212: Potential role for DYRK as a glycogen synthase kinase 3-priming kinase. Biochem. J. 355, 609-615
    • (2001) Biochem. J. , vol.355 , pp. 609-615
    • Woods, Y.L.1    Cohen, P.2    Becker, W.3    Jakes, R.4    Goedert, M.5    Wang, X.6    Proud, C.G.7
  • 41
    • 1642535438 scopus 로고    scopus 로고
    • Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases
    • Skurat, A. V. and Dietrich, A. D. (2004) Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases. J. Biol. Chem. 279, 2490-2498
    • (2004) J. Biol. Chem. , vol.279 , pp. 2490-2498
    • Skurat, A.V.1    Dietrich, A.D.2
  • 42
    • 69249110053 scopus 로고    scopus 로고
    • Mirk regulates the exit of colon cancer cells from quiescence
    • Jin, K., Ewton, D. Z., Park, S., Hu, J. and Friedman, E. (2009) Mirk regulates the exit of colon cancer cells from quiescence. J. Biol. Chem. 284, 22916-22925
    • (2009) J. Biol. Chem. , vol.284 , pp. 22916-22925
    • Jin, K.1    Ewton, D.Z.2    Park, S.3    Hu, J.4    Friedman, E.5
  • 43
    • 0034616913 scopus 로고    scopus 로고
    • Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage
    • Agami, R. and Bernards, R. (2000) Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage. Cell 102, 55-66
    • (2000) Cell , vol.102 , pp. 55-66
    • Agami, R.1    Bernards, R.2
  • 44
    • 70350316226 scopus 로고    scopus 로고
    • Mirk/Dyrk1B, a novel therapeutic target, mediates cell survival in non-small cell lung cancer cells
    • Gao, J., Zheng, Z., Rawal, B., Schell, M. J., Bepler, G. and Haura, E. B. (2009) Mirk/Dyrk1B, a novel therapeutic target, mediates cell survival in non-small cell lung cancer cells. Cancer Biol. Ther. 8, 1671-1679
    • (2009) Cancer Biol. Ther. , vol.8 , pp. 1671-1679
    • Gao, J.1    Zheng, Z.2    Rawal, B.3    Schell, M.J.4    Bepler, G.5    Haura, E.B.6
  • 45
    • 65949118505 scopus 로고    scopus 로고
    • Mirk/Dyrk1B maintains the viability of quiescent pancreatic cancer cells by reducing levels of reactive oxygen species
    • Deng, X., Ewton, D. Z. and Friedman, E. (2009) Mirk/Dyrk1B maintains the viability of quiescent pancreatic cancer cells by reducing levels of reactive oxygen species. Cancer Res. 69, 3317-3324
    • (2009) Cancer Res , vol.69 , pp. 3317-3324
    • Deng, X.1    Ewton, D.Z.2    Friedman, E.3


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