메뉴 건너뛰기




Volumn 92, Issue 10, 2012, Pages 1503-1514

Dissecting the phenotypes of Plk1 inhibition in cancer cells using novel kinase inhibitory chemical CBB2001

Author keywords

Aurora kinase; CBB2001; geminin; mitosis; Plk1 kinase

Indexed keywords

2 CYANO N (2,5 DIBROMOPHENYL) 3 HYDROXYCROTONAMIDE; ANTINEOPLASTIC AGENT; AURORA A KINASE; AURORA KINASE INHIBITOR; CBB 2001; CYCLIN B1; GEMININ; POLO LIKE KINASE 1; RIGOSERTIB; UNCLASSIFIED DRUG;

EID: 84866840285     PISSN: 00236837     EISSN: 15300307     Source Type: Journal    
DOI: 10.1038/labinvest.2012.114     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 33645316142 scopus 로고    scopus 로고
    • Targeting polo-like kinase 1 for cancer therapy
    • Strebhardt K, Ullrich A. Targeting polo-like kinase 1 for cancer therapy. Nat Rev Cancer 2006;6:321-330.
    • (2006) Nat Rev Cancer , vol.6 , pp. 321-330
    • Strebhardt, K.1    Ullrich, A.2
  • 2
    • 2942615282 scopus 로고    scopus 로고
    • Polo-like kinases and the orchestration of cell division
    • Barr FA, Sillje HH, Nigg EA. Polo-like kinases and the orchestration of cell division. Nat Rev Mol Cell Biol 2004;5:429-440.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 429-440
    • Barr, F.A.1    Sillje, H.H.2    Nigg, E.A.3
  • 3
    • 33746869956 scopus 로고    scopus 로고
    • Polo-like kinase 1: Target and regulator of anaphase-promoting complex/cyclosome-dependent proteolysis
    • Eckerdt F, Strebhardt K. Polo-like kinase 1: target and regulator of anaphase-promoting complex/cyclosome-dependent proteolysis. Cancer Res 2006;66:6895-6898.
    • (2006) Cancer Res , vol.66 , pp. 6895-6898
    • Eckerdt, F.1    Strebhardt, K.2
  • 4
    • 2542617641 scopus 로고    scopus 로고
    • Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome
    • Moshe Y, Boulaire J, Pagano M, et al. Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome. Proc Natl Acad Sci USA 2004;101: 7937-7942.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7937-7942
    • Moshe, Y.1    Boulaire, J.2    Pagano, M.3
  • 5
    • 0038492408 scopus 로고    scopus 로고
    • Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate
    • Nakajima H, Toyoshima-Morimoto F, Taniguchi E, et al. Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate. J Biol Chem 2003;278:25277-25280.
    • (2003) J Biol Chem , vol.278 , pp. 25277-25280
    • Nakajima, H.1    Toyoshima-Morimoto, F.2    Taniguchi, E.3
  • 6
    • 0036256260 scopus 로고    scopus 로고
    • Plk1 promotes nuclear translocation of human Cdc25C during prophase
    • Toyoshima-Morimoto F, Taniguchi E, Nishida E. Plk1 promotes nuclear translocation of human Cdc25C during prophase. EMBO Rep 2002; 3:341-348.
    • (2002) EMBO Rep , vol.3 , pp. 341-348
    • Toyoshima-Morimoto, F.1    Taniguchi, E.2    Nishida, E.3
  • 7
    • 0029079267 scopus 로고
    • Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function
    • Golsteyn RM, Mundt KE, Fry AM, et al. Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function. J Cell Biol 1995;129:1617-1628.
    • (1995) J Cell Biol , vol.129 , pp. 1617-1628
    • Golsteyn, R.M.1    Mundt, K.E.2    Fry, A.M.3
  • 8
    • 33749165420 scopus 로고    scopus 로고
    • The Plk1 target Kizuna stabilizes mitotic centrosomes to ensure spindle bipolarity
    • Oshimori N, Ohsugi M, Yamamoto T. The Plk1 target Kizuna stabilizes mitotic centrosomes to ensure spindle bipolarity. Nat Cell Biol 2006;8:1095-1101.
    • (2006) Nat Cell Biol , vol.8 , pp. 1095-1101
    • Oshimori, N.1    Ohsugi, M.2    Yamamoto, T.3
  • 9
    • 33845981777 scopus 로고    scopus 로고
    • PICH a centromere-associated SNF2 family ATPase, is regulated by Plk1 and required for the spindle checkpoint
    • Baumann C, Korner R, Hofmann K, et al. PICH a centromere-associated SNF2 family ATPase, is regulated by Plk1 and required for the spindle checkpoint. Cell 2007;128:101-114.
    • (2007) Cell , vol.128 , pp. 101-114
    • Baumann, C.1    Korner, R.2    Hofmann, K.3
  • 10
    • 34548276583 scopus 로고    scopus 로고
    • Shugoshin 1 plays a central role in kinetochore assembly and is required for kinetochore targeting of Plk1
    • Pouwels J, Kukkonen AM, Lan W, et al. Shugoshin 1 plays a central role in kinetochore assembly and is required for kinetochore targeting of Plk1. Cell Cycle 2007;6:1579-1585.
    • (2007) Cell Cycle , vol.6 , pp. 1579-1585
    • Pouwels, J.1    Kukkonen, A.M.2    Lan, W.3
  • 11
    • 77950669409 scopus 로고    scopus 로고
    • PICH and cotargeted Plk1 coordinately maintain prometaphase chromosome arm architecture
    • Kurasawa Y, Yu-Lee LY. PICH and cotargeted Plk1 coordinately maintain prometaphase chromosome arm architecture. Mol Biol Cell 2010;21:1188-1199.
    • (2010) Mol Biol Cell , vol.21 , pp. 1188-1199
    • Kurasawa, Y.1    Yu-Lee, L.Y.2
  • 12
    • 41149134864 scopus 로고    scopus 로고
    • Role for Plk1 phosphorylation of Hbo1 in regulation of replication licensing
    • Wu ZQ, Liu X. Role for Plk1 phosphorylation of Hbo1 in regulation of replication licensing. Proc Natl Acad Sci USA 2008;105:1919-1924.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1919-1924
    • Wu, Z.Q.1    Liu, X.2
  • 13
    • 0037648703 scopus 로고    scopus 로고
    • Polo-like kinase 1 (PLK1) is overexpressed in primary colorectal cancers
    • Takahashi T, Sano B, Nagata T, et al. Polo-like kinase 1 (PLK1) is overexpressed in primary colorectal cancers. Cancer Sci 2003;94:148-152.
    • (2003) Cancer Sci , vol.94 , pp. 148-152
    • Takahashi, T.1    Sano, B.2    Nagata, T.3
  • 14
    • 33746622832 scopus 로고    scopus 로고
    • Overexpression of pololike kinase 1 (PLK1) and chromosomal instability in bladder cancer
    • Yamamoto Y, Matsuyama H, Kawauchi S, et al. Overexpression of pololike kinase 1 (PLK1) and chromosomal instability in bladder cancer. Oncology 2006;70:231-237.
    • (2006) Oncology , vol.70 , pp. 231-237
    • Yamamoto, Y.1    Matsuyama, H.2    Kawauchi, S.3
  • 15
    • 68049112546 scopus 로고    scopus 로고
    • Polo-like kinase (PLK) inhibitors in preclinical and early clinical development in oncology
    • Schoffski P. Polo-like kinase (PLK) inhibitors in preclinical and early clinical development in oncology. Oncologist 2009;14:559-570.
    • (2009) Oncologist , vol.14 , pp. 559-570
    • Schoffski, P.1
  • 16
    • 33646811208 scopus 로고    scopus 로고
    • Expression of polo-like kinase 1 (PLK1) protein predicts the survival of patients with gastric carcinoma
    • Kanaji S, Saito H, Tsujitani S, et al. Expression of polo-like kinase 1 (PLK1) protein predicts the survival of patients with gastric carcinoma. Oncology 2006;70:126-133.
    • (2006) Oncology , vol.70 , pp. 126-133
    • Kanaji, S.1    Saito, H.2    Tsujitani, S.3
  • 17
    • 0037172998 scopus 로고    scopus 로고
    • Activation of Cdc2/cyclin B and inhibition of centrosome amplification in cells depleted of Plk1 by siRNA
    • Liu X, Erikson RL. Activation of Cdc2/cyclin B and inhibition of centrosome amplification in cells depleted of Plk1 by siRNA. Proc Natl Acad Sci USA 2002;99:8672-8676.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8672-8676
    • Liu, X.1    Erikson, R.L.2
  • 18
    • 16844369144 scopus 로고    scopus 로고
    • Small interfering RNA-mediated Polo-like kinase 1 depletion preferentially reduces the survival of p53-defective, oncogenic transformed cells and inhibits tumor growth in animals
    • Guan R, Tapang P, Leverson JD, et al. Small interfering RNA-mediated Polo-like kinase 1 depletion preferentially reduces the survival of p53-defective, oncogenic transformed cells and inhibits tumor growth in animals. Cancer Res 2005;65:2698-2704.
    • (2005) Cancer Res , vol.65 , pp. 2698-2704
    • Guan, R.1    Tapang, P.2    Leverson, J.D.3
  • 19
    • 51349144633 scopus 로고    scopus 로고
    • Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery
    • Macurek L, Lindqvist A, Lim D, et al. Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery. Nature 2008;455:119-123.
    • (2008) Nature , vol.455 , pp. 119-123
    • MacUrek, L.1    Lindqvist, A.2    Lim, D.3
  • 20
    • 46249084662 scopus 로고    scopus 로고
    • Bora and the kinase Aurora a cooperatively activate the kinase Plk1 and control mitotic entry
    • Seki A, Coppinger JA, Jang CY, et al. Bora and the kinase Aurora a cooperatively activate the kinase Plk1 and control mitotic entry. Science 2008;320:1655-1658.
    • (2008) Science , vol.320 , pp. 1655-1658
    • Seki, A.1    Coppinger, J.A.2    Jang, C.Y.3
  • 21
    • 10344236486 scopus 로고    scopus 로고
    • Aurora-kinase inhibitors as anticancer agents
    • Keen N, Taylor S. Aurora-kinase inhibitors as anticancer agents. Nat Rev Cancer 2004;4:927-936.
    • (2004) Nat Rev Cancer , vol.4 , pp. 927-936
    • Keen, N.1    Taylor, S.2
  • 22
    • 39149089275 scopus 로고    scopus 로고
    • Polo and Aurora kinases: Lessons derived from chemical biology
    • Taylor S, Peters JM. Polo and Aurora kinases: lessons derived from chemical biology. Curr Opin Cell Biol 2008;20:77-84.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 77-84
    • Taylor, S.1    Peters, J.M.2
  • 23
    • 0037084163 scopus 로고    scopus 로고
    • Aurora-A overexpression reveals tetraploidization as a major route to centrosome amplification in p53 cells
    • Meraldi P, Honda R, Nigg EA. Aurora-A overexpression reveals tetraploidization as a major route to centrosome amplification in p53 cells. EMBO J 2002;21:483-492.
    • (2002) EMBO J , vol.21 , pp. 483-492
    • Meraldi, P.1    Honda, R.2    Nigg, E.A.3
  • 24
    • 0032100685 scopus 로고    scopus 로고
    • A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers
    • Bischoff JR, Anderson L, Zhu Y, et al. A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers. EMBO J 1998;17:3052-3065.
    • (1998) EMBO J , vol.17 , pp. 3052-3065
    • Bischoff, J.R.1    Anderson, L.2    Zhu, Y.3
  • 25
    • 64749095806 scopus 로고    scopus 로고
    • Geminin is partially localized to the centrosome and plays a role in proper centrosome duplication
    • Lu F, Lan R, Zhang H, et al. Geminin is partially localized to the centrosome and plays a role in proper centrosome duplication. Biol Cell 2009;101:273-285.
    • (2009) Biol Cell , vol.101 , pp. 273-285
    • Lu, F.1    Lan, R.2    Zhang, H.3
  • 26
    • 33645828666 scopus 로고    scopus 로고
    • Nocodazole does not synchronize cells: Implications for cell-cycle control and whole-culture synchronization
    • Cooper S, Iyer G, Tarquini M, et al. Nocodazole does not synchronize cells: implications for cell-cycle control and whole-culture synchronization. Cell Tissue Res 2006;324:237-242.
    • (2006) Cell Tissue Res , vol.324 , pp. 237-242
    • Cooper, S.1    Iyer, G.2    Tarquini, M.3
  • 27
    • 61649121756 scopus 로고    scopus 로고
    • Design of potent thiophene inhibitors of polo-like kinase 1 with improved solubility and reduced protein binding
    • Emmitte KA, Adjabeng GM, Andrews CW, et al. Design of potent thiophene inhibitors of polo-like kinase 1 with improved solubility and reduced protein binding. Bioorg Med Chem Lett 2009;19: 1694-1697.
    • (2009) Bioorg Med Chem Lett , vol.19 , pp. 1694-1697
    • Emmitte, K.A.1    Adjabeng, G.M.2    Andrews, C.W.3
  • 28
    • 33747831132 scopus 로고    scopus 로고
    • L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage
    • Higa LA, Banks D, Wu M, et al. L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage. Cell Cycle 2006;5:1675-1680.
    • (2006) Cell Cycle , vol.5 , pp. 1675-1680
    • Higa, L.A.1    Banks, D.2    Wu, M.3
  • 29
    • 0242525214 scopus 로고    scopus 로고
    • Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint
    • Higa LA, Mihaylov IS, Banks DP, et al. Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint. Nat Cell Biol 2003;5:1008-1015.
    • (2003) Nat Cell Biol , vol.5 , pp. 1008-1015
    • Higa, L.A.1    Mihaylov, I.S.2    Banks, D.P.3
  • 30
    • 33750509178 scopus 로고    scopus 로고
    • CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation
    • Higa LA, Wu M, Ye T, et al. CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation. Nat Cell Biol 2006;8:1277-1283.
    • (2006) Nat Cell Biol , vol.8 , pp. 1277-1283
    • Higa, L.A.1    Wu, M.2    Ye, T.3
  • 31
    • 0038624074 scopus 로고    scopus 로고
    • Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells
    • Liu X, Erikson RL. Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells. Proc Natl Acad Sci USA 2003;100:5789-5794.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5789-5794
    • Liu, X.1    Erikson, R.L.2
  • 32
    • 38849198696 scopus 로고    scopus 로고
    • Cyclin B1 is localized to unattached kinetochores and contributes to efficient microtubule attachment and proper chromosome alignment during mitosis
    • Chen Q, Zhang X, Jiang Q, et al. Cyclin B1 is localized to unattached kinetochores and contributes to efficient microtubule attachment and proper chromosome alignment during mitosis. Cell Res 2008;18: 268-280.
    • (2008) Cell Res , vol.18 , pp. 268-280
    • Chen, Q.1    Zhang, X.2    Jiang, Q.3
  • 33
    • 33846931644 scopus 로고    scopus 로고
    • The small-molecule inhibitor BI 2536 reveals novel insights into mitotic roles of polo-like kinase 1
    • Lenart P, Petronczki M, Steegmaier M, et al. The small-molecule inhibitor BI 2536 reveals novel insights into mitotic roles of polo-like kinase 1. Curr Biol 2007;17:304-315.
    • (2007) Curr Biol , vol.17 , pp. 304-315
    • Lenart, P.1    Petronczki, M.2    Steegmaier, M.3
  • 34
    • 34548058372 scopus 로고    scopus 로고
    • Pharmacological and functional comparison of the polo-like kinase family: Insight into inhibitor and substrate specificity
    • Johnson EF, Stewart KD, Woods KW, et al. Pharmacological and functional comparison of the polo-like kinase family: insight into inhibitor and substrate specificity. Biochemistry 2007;46:9551-9563.
    • (2007) Biochemistry , vol.46 , pp. 9551-9563
    • Johnson, E.F.1    Stewart, K.D.2    Woods, K.W.3
  • 35
    • 34347254640 scopus 로고    scopus 로고
    • Establishment of human tumor xenografts in immunodeficient mice
    • Morton CL, Houghton PJ. Establishment of human tumor xenografts in immunodeficient mice. Nat Protoc 2007;2:247-250.
    • (2007) Nat Protoc , vol.2 , pp. 247-250
    • Morton, C.L.1    Houghton, P.J.2
  • 36
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O, Olson AJ. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 2010;31:455-461.
    • (2010) J Comput Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 37
    • 34249076619 scopus 로고    scopus 로고
    • Structure of the catalytic domain of human polo-like kinase 1
    • Kothe M, Kohls D, Low S, et al. Structure of the catalytic domain of human polo-like kinase 1. Biochemistry 2007;46:5960-5971.
    • (2007) Biochemistry , vol.46 , pp. 5960-5971
    • Kothe, M.1    Kohls, D.2    Low, S.3
  • 38
    • 77954600984 scopus 로고    scopus 로고
    • Genetic approach to evaluate specificity of small molecule drug candidates inhibiting PLK1 using zebrafish
    • Zhong H, Xin S, Zhao Y, et al. Genetic approach to evaluate specificity of small molecule drug candidates inhibiting PLK1 using zebrafish. Mol Biosyst, 6:1463-1468.
    • Mol Biosyst , vol.6 , pp. 1463-1468
    • Zhong, H.1    Xin, S.2    Zhao, Y.3
  • 39
    • 68249137199 scopus 로고    scopus 로고
    • Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1
    • Yun SM, Moulaei T, Lim D, et al. Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1. Nat Struct Mol Biol 2009;16:876-882.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 876-882
    • Yun, S.M.1    Moulaei, T.2    Lim, D.3
  • 40
    • 1642378661 scopus 로고    scopus 로고
    • Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase
    • Bashir T, Dorrello NV, Amador V, et al. Control of the SCF(Skp2-Cks1) ubiquitin ligase by the APC/C(Cdh1) ubiquitin ligase. Nature 2004;428:190-193.
    • (2004) Nature , vol.428 , pp. 190-193
    • Bashir, T.1    Dorrello, N.V.2    Amador, V.3
  • 41
    • 1642399624 scopus 로고    scopus 로고
    • Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex
    • Wei W, Ayad NG, Wan Y, et al. Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex. Nature 2004;428:194-198.
    • (2004) Nature , vol.428 , pp. 194-198
    • Wei, W.1    Ayad, N.G.2    Wan, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.