메뉴 건너뛰기




Volumn 34, Issue 37, 2015, Pages 4799-4807

Understanding the Polo Kinase machine

Author keywords

[No Author keywords available]

Indexed keywords

POLO LIKE KINASE; CELL CYCLE PROTEIN; MULTIPROTEIN COMPLEX; ONCOPROTEIN; POLO-LIKE KINASE 1; PROTEIN SERINE THREONINE KINASE;

EID: 84941314826     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2014.451     Document Type: Review
Times cited : (119)

References (121)
  • 1
    • 0023804548 scopus 로고
    • Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles
    • Sunkel CE, Glover DM. Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles. J Cell Sci 1988; 89: 25-38.
    • (1988) J Cell Sci , vol.89 , pp. 25-38
    • Sunkel, C.E.1    Glover, D.M.2
  • 3
    • 62849123093 scopus 로고    scopus 로고
    • Polo-like kinases: Conservation and divergence in their functions and regulation
    • Archambault V, Glover DM. Polo-like kinases: conservation and divergence in their functions and regulation. Nat Rev Mol Cell Biol 2009; 10: 265-275.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 265-275
    • Archambault, V.1    Glover, D.M.2
  • 5
    • 0015847513 scopus 로고
    • Genetic control of the cell division cycle in yeast: V. Genetic analysis of CDC mutants
    • Hartwell LH, Mortimer RK, Culotti J, Culotti M. Genetic Control of the Cell Division Cycle in Yeast: V. Genetic Analysis of cdc Mutants. Genetics 1973; 74: 267-286.
    • (1973) Genetics , vol.74 , pp. 267-286
    • Hartwell, L.H.1    Mortimer, R.K.2    Culotti, J.3    Culotti, M.4
  • 6
    • 0032482986 scopus 로고    scopus 로고
    • Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk
    • Lee KS, Grenfell TZ, Yarm FR, Erikson RL. Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk. Proc Natl Acad Sci USA 1998; 95: 9301-9306.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9301-9306
    • Lee, K.S.1    Grenfell, T.Z.2    Yarm, F.R.3    Erikson, R.L.4
  • 7
    • 0242515843 scopus 로고    scopus 로고
    • Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates
    • Elia AE, Cantley LC, Yaffe MB. Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates. Science 2003; 299: 1228-1231.
    • (2003) Science , vol.299 , pp. 1228-1231
    • Elia, A.E.1    Cantley, L.C.2    Yaffe, M.B.3
  • 8
    • 10744221449 scopus 로고    scopus 로고
    • The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain
    • Elia AE, Rellos P, Haire LF, Chao JW, Ivins FJ, Hoepker K et al. The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain. Cell 2003; 115: 83-95.
    • (2003) Cell , vol.115 , pp. 83-95
    • Elia, A.E.1    Rellos, P.2    Haire, L.F.3    Chao, J.W.4    Ivins, F.J.5    Hoepker, K.6
  • 9
    • 79960446938 scopus 로고    scopus 로고
    • From Plk1 to Plk5: Functional evolution of polo-like kinases
    • de Carcer G, Manning G, Malumbres M. From Plk1 to Plk5: functional evolution of polo-like kinases. Cell Cycle 2011; 10: 2255-2262.
    • (2011) Cell Cycle , vol.10 , pp. 2255-2262
    • De Carcer, G.1    Manning, G.2    Malumbres, M.3
  • 11
    • 0030462914 scopus 로고    scopus 로고
    • Antibody microinjection reveals an essential role for human polo-like kinase 1 (Plk1) in the functional maturation of mitotic centrosomes
    • Lane HA, Nigg EA. Antibody microinjection reveals an essential role for human polo-like kinase 1 (Plk1) in the functional maturation of mitotic centrosomes. J Cell Biol 1996; 135: 1701-1713.
    • (1996) J Cell Biol , vol.135 , pp. 1701-1713
    • Lane, H.A.1    Nigg, E.A.2
  • 13
    • 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, Nigg EA. 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    Nigg, E.A.4
  • 15
    • 34548436939 scopus 로고    scopus 로고
    • Tension-sensitive Plk1 phosphorylation on BubR1 regulates the stability of kinetochore microtubule interactions
    • Elowe S, Hummer S, Uldschmid A, Li X, Nigg EA. Tension-sensitive Plk1 phosphorylation on BubR1 regulates the stability of kinetochore microtubule interactions. Genes Dev 2007; 21: 2205-2219.
    • (2007) Genes Dev , vol.21 , pp. 2205-2219
    • Elowe, S.1    Hummer, S.2    Uldschmid, A.3    Li, X.4    Nigg, E.A.5
  • 16
    • 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, Di Fiore B, Lipp JJ, Hoffmann 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    Di Fiore, B.4    Lipp, J.J.5    Hoffmann, M.6
  • 17
    • 84904568486 scopus 로고    scopus 로고
    • Polo-like kinase 1 licenses CENP-A deposition at centromeres
    • McKinley KL, Cheeseman IM. Polo-like kinase 1 licenses CENP-A deposition at centromeres. Cell 2014; 158: 397-411.
    • (2014) Cell , vol.158 , pp. 397-411
    • McKinley, K.L.1    Cheeseman, I.M.2
  • 18
    • 34047119210 scopus 로고    scopus 로고
    • Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1
    • Neef R, Gruneberg U, Kopajtich R, Li X, Nigg EA, Sillje H et al. Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1. Nat Cell Biol 2007; 9: 436-444.
    • (2007) Nat Cell Biol , vol.9 , pp. 436-444
    • Neef, R.1    Gruneberg, U.2    Kopajtich, R.3    Li, X.4    Nigg, E.A.5    Sillje, H.6
  • 19
    • 34247578600 scopus 로고    scopus 로고
    • Chemical genetics reveals the requirement for Polo-like kinase 1 activity in positioning RhoA and triggering cytokinesis in human cells
    • Burkard ME, Randall CL, Larochelle S, Zhang C, Shokat KM, Fisher RP et al. Chemical genetics reveals the requirement for Polo-like kinase 1 activity in positioning RhoA and triggering cytokinesis in human cells. Proc Natl Acad Sci USA 2007; 104: 4383-4388.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4383-4388
    • Burkard, M.E.1    Randall, C.L.2    Larochelle, S.3    Zhang, C.4    Shokat, K.M.5    Fisher, R.P.6
  • 20
    • 55849140477 scopus 로고    scopus 로고
    • Polo-like kinase controls vertebrate spindle elongation and cytokinesis
    • Brennan IM, Peters U, Kapoor TM, Straight AF. Polo-like kinase controls vertebrate spindle elongation and cytokinesis. PLoS One 2007; 2: e409.
    • (2007) PLoS One , vol.2 , pp. e409
    • Brennan, I.M.1    Peters, U.2    Kapoor, T.M.3    Straight, A.F.4
  • 21
    • 34247611900 scopus 로고    scopus 로고
    • Polo-like kinase 1 triggers the initiation of cytokinesis in human cells by promoting recruitment of the RhoGEF Ect2 to the central spindle
    • Petronczki M, Glotzer M, Kraut N, Peters JM. Polo-like kinase 1 triggers the initiation of cytokinesis in human cells by promoting recruitment of the RhoGEF Ect2 to the central spindle. Dev Cell 2007; 12: 713-725.
    • (2007) Dev Cell , vol.12 , pp. 713-725
    • Petronczki, M.1    Glotzer, M.2    Kraut, N.3    Peters, J.M.4
  • 22
    • 34948818671 scopus 로고    scopus 로고
    • Use of the novel Plk1 inhibitor ZK-thiazolidinone to elucidate functions of Plk1 in early and late stages of mitosis
    • Santamaria A, Neef R, Eberspacher U, Eis K, Husemann M, Mumberg D et al. Use of the novel Plk1 inhibitor ZK-thiazolidinone to elucidate functions of Plk1 in early and late stages of mitosis. Mol Biol Cell 2007; 18: 4024-4036.
    • (2007) Mol Biol Cell , vol.18 , pp. 4024-4036
    • Santamaria, A.1    Neef, R.2    Eberspacher, U.3    Eis, K.4    Husemann, M.5    Mumberg, D.6
  • 23
    • 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
  • 24
    • 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, Yates JR, Fang G. 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    Yates, J.R.4    Fang, G.5
  • 25
    • 0036209010 scopus 로고    scopus 로고
    • The dissociation of cohesin from chromosomes in prophase is regulated by Polo-like kinase
    • Sumara I, Vorlaufer E, Stukenberg PT, Kelm O, Redemann N, Nigg EA et al. The dissociation of cohesin from chromosomes in prophase is regulated by Polo-like kinase. Mol Cell 2002; 9: 515-525.
    • (2002) Mol Cell , vol.9 , pp. 515-525
    • Sumara, I.1    Vorlaufer, E.2    Stukenberg, P.T.3    Kelm, O.4    Redemann, N.5    Nigg, E.A.6
  • 26
    • 79955393903 scopus 로고    scopus 로고
    • The initial phase of chromosome condensation requires Cdk1-mediated phosphorylation of the CAP-D3 subunit of condensin II
    • Abe S, Nagasaka K, Hirayama Y, Kozuka-Hata H, Oyama M, Aoyagi Y et al. The initial phase of chromosome condensation requires Cdk1-mediated phosphorylation of the CAP-D3 subunit of condensin II. Genes Dev 2011; 25: 863-874.
    • (2011) Genes Dev , vol.25 , pp. 863-874
    • Abe, S.1    Nagasaka, K.2    Hirayama, Y.3    Kozuka-Hata, H.4    Oyama, M.5    Aoyagi, Y.6
  • 31
    • 33846904706 scopus 로고    scopus 로고
    • Polo-like kinase 3 is required for entry into S phase
    • Zimmerman WC, Erikson RL. Polo-like kinase 3 is required for entry into S phase. Proc Natl Acad Sci USA 2007; 104: 1847-1852.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1847-1852
    • Zimmerman, W.C.1    Erikson, R.L.2
  • 32
    • 0042132030 scopus 로고    scopus 로고
    • Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic catastrophe in paclitaxel (taxol)-exposed cells
    • Burns TF, Fei P, Scata KA, Dicker DT, El-Deiry WS. Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic catastrophe in paclitaxel (taxol)-exposed cells. Mol Cell Biol 2003; 23: 5556-5571.
    • (2003) Mol Cell Biol , vol.23 , pp. 5556-5571
    • Burns, T.F.1    Fei, P.2    Scata, K.A.3    Dicker, D.T.4    El-Deiry, W.S.5
  • 33
    • 35848966121 scopus 로고    scopus 로고
    • Replication stress, defective S-phase checkpoint and increased death in Plk2-deficient human cancer cells
    • Matthew EM, Yen TJ, Dicker DT, Dorsey JF, Yang W, Navaraj A et al. Replication stress, defective S-phase checkpoint and increased death in Plk2-deficient human cancer cells. Cell Cycle 2007; 6: 2571-2578.
    • (2007) Cell Cycle , vol.6 , pp. 2571-2578
    • Matthew, E.M.1    Yen, T.J.2    Dicker, D.T.3    Dorsey, J.F.4    Yang, W.5    Navaraj, A.6
  • 34
    • 0035900745 scopus 로고    scopus 로고
    • Plk3 functionally links DNA damage to cell cycle arrest and apoptosis at least in part via the p53 pathway
    • Xie S, Wu H, Wang Q, Cogswell JP, Husain I, Conn C et al. Plk3 functionally links DNA damage to cell cycle arrest and apoptosis at least in part via the p53 pathway. J Biol Chem 2001; 276: 43305-43312.
    • (2001) J Biol Chem , vol.276 , pp. 43305-43312
    • Xie, S.1    Wu, H.2    Wang, Q.3    Cogswell, J.P.4    Husain, I.5    Conn, C.6
  • 35
    • 0037179845 scopus 로고    scopus 로고
    • Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein involved in stress response pathways
    • Bahassi el M, Conn CW, Myer DL, Hennigan RF, McGowan CH, Sanchez Y et al. Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein involved in stress response pathways. Oncogene 2002; 21: 6633-6640.
    • (2002) Oncogene , vol.21 , pp. 6633-6640
    • Bahassiel, M.1    Conn, C.W.2    Myer, D.L.3    Hennigan, R.F.4    McGowan, C.H.5    Sanchez, Y.6
  • 36
    • 13044313478 scopus 로고    scopus 로고
    • The polo-like protein kinases Fnk and Snk associate with a Ca(2+)-and integrin-binding protein and are regulated dynamically with synaptic plasticity
    • Kauselmann G, Weiler M, Wulff P, Jessberger S, Konietzko U, Scafidi J et al. The polo-like protein kinases Fnk and Snk associate with a Ca(2+)-and integrin-binding protein and are regulated dynamically with synaptic plasticity. EMBO J 1999; 18: 5528-5539.
    • (1999) EMBO J , vol.18 , pp. 5528-5539
    • Kauselmann, G.1    Weiler, M.2    Wulff, P.3    Jessberger, S.4    Konietzko, U.5    Scafidi, J.6
  • 37
    • 43649097642 scopus 로고    scopus 로고
    • Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity
    • Seeburg DP, Feliu-Mojer M, Gaiottino J, Pak DT, Sheng M. Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity. Neuron 2008; 58: 571-583.
    • (2008) Neuron , vol.58 , pp. 571-583
    • Seeburg, D.P.1    Feliu-Mojer, M.2    Gaiottino, J.3    Pak, D.T.4    Sheng, M.5
  • 38
    • 79952263859 scopus 로고    scopus 로고
    • Plk5, a polo box domain-only protein with specific roles in neuron differentiation and glioblastoma suppression
    • de Carcer G, Escobar B, Higuero AM, Garcia L, Anson A, Perez G et al. Plk5, a polo box domain-only protein with specific roles in neuron differentiation and glioblastoma suppression. Mol Cell Biol 2011; 31: 1225-1239.
    • (2011) Mol Cell Biol , vol.31 , pp. 1225-1239
    • De Carcer, G.1    Escobar, B.2    Higuero, A.M.3    Garcia, L.4    Anson, A.5    Perez, G.6
  • 40
    • 43049151493 scopus 로고    scopus 로고
    • Polo on the Rise-from Mitotic Entry to Cytokinesis with Plk1
    • Petronczki M, Lenart P, Peters JM. Polo on the Rise-from Mitotic Entry to Cytokinesis with Plk1. Dev Cell 2008; 14: 646-659.
    • (2008) Dev Cell , vol.14 , pp. 646-659
    • Petronczki, M.1    Lenart, P.2    Peters, J.M.3
  • 41
    • 77955167321 scopus 로고    scopus 로고
    • Multifaceted polo-like kinases: Drug targets and antitargets for cancer therapy
    • Strebhardt K. Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy. Nat Rev Drug Discov 2010; 9: 643-660.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 643-660
    • Strebhardt, K.1
  • 42
    • 84855676685 scopus 로고    scopus 로고
    • Plk1-targeted small molecule inhibitors: Molecular basis for their potency and specificity
    • Murugan RN, Park JE, Kim EH, Shin SY, Cheong C, Lee KS et al. Plk1-targeted small molecule inhibitors: molecular basis for their potency and specificity. Mol Cells 2011; 32: 209-220.
    • (2011) Mol Cells , vol.32 , pp. 209-220
    • Murugan, R.N.1    Park, J.E.2    Kim, E.H.3    Shin, S.Y.4    Cheong, C.5    Lee, K.S.6
  • 43
    • 84920698054 scopus 로고    scopus 로고
    • Discovery and development of the Polo-like kinase inhibitor volasertib in cancer therapy
    • Gjertsen BT, Schoffski P. Discovery and development of the Polo-like kinase inhibitor volasertib in cancer therapy. Leukemia 2015; 29: 11-19.
    • (2015) Leukemia , vol.29 , pp. 11-19
    • Gjertsen, B.T.1    Schoffski, P.2
  • 44
    • 0037133203 scopus 로고    scopus 로고
    • Functional studies on the role of the C-terminal domain of mammalian polo-like kinase
    • Jang YJ, Lin CY, Ma S, Erikson RL. Functional studies on the role of the C-terminal domain of mammalian polo-like kinase. Proc Natl Acad Sci USA 2002; 99: 1984-1989.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1984-1989
    • Jang, Y.J.1    Lin, C.Y.2    Ma, S.3    Erikson, R.L.4
  • 45
    • 0242556820 scopus 로고    scopus 로고
    • The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex
    • Cheng KY, Lowe ED, Sinclair J, Nigg EA, Johnson LN. The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex. EMBO J 2003; 22: 5757-5768.
    • (2003) EMBO J , vol.22 , pp. 5757-5768
    • Cheng, K.Y.1    Lowe, E.D.2    Sinclair, J.3    Nigg, E.A.4    Johnson, L.N.5
  • 46
    • 13244284602 scopus 로고    scopus 로고
    • Structure and function of Polo-like kinases
    • Lowery DM, Lim D, Yaffe MB. Structure and function of Polo-like kinases. Oncogene 2005; 24: 248-259.
    • (2005) Oncogene , vol.24 , pp. 248-259
    • Lowery, D.M.1    Lim, D.2    Yaffe, M.B.3
  • 48
    • 0037073722 scopus 로고    scopus 로고
    • Nuclear translocation of plk1 mediated by its bipartite nuclear localization signal
    • Taniguchi E, Toyoshima-Morimoto F, Nishida E. Nuclear translocation of plk1 mediated by its bipartite nuclear localization signal. J Biol Chem 2002; 277: 48884-48888.
    • (2002) J Biol Chem , vol.277 , pp. 48884-48888
    • Taniguchi, E.1    Toyoshima-Morimoto, F.2    Nishida, E.3
  • 49
    • 0031581099 scopus 로고    scopus 로고
    • On the regulation and function of human polo-like kinase 1 (PLK1): Effects of overexpression on cell cycle progression
    • Mundt KE, Golsteyn RM, Lane HA, Nigg EA. On the regulation and function of human polo-like kinase 1 (PLK1): effects of overexpression on cell cycle progression. Biochem Biophys Res Commun 1997; 239: 377-385.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 377-385
    • Mundt, K.E.1    Golsteyn, R.M.2    Lane, H.A.3    Nigg, E.A.4
  • 50
    • 84883740937 scopus 로고    scopus 로고
    • Structural basis for the inhibition of Polo-like kinase 1
    • Xu J, Shen C, Wang T, Quan J. Structural basis for the inhibition of Polo-like kinase 1. Nat Struct Mol Biol 2013; 20: 1047-1053.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 1047-1053
    • Xu, J.1    Shen, C.2    Wang, T.3    Quan, J.4
  • 51
    • 53549131982 scopus 로고    scopus 로고
    • Sequestration of Polo kinase to microtubules by phosphopriming-independent binding to Map205 is relieved by phosphorylation at a CDK site in mitosis
    • Archambault V, D'Avino PP, Deery MJ, Lilley KS, Glover DM. Sequestration of Polo kinase to microtubules by phosphopriming-independent binding to Map205 is relieved by phosphorylation at a CDK site in mitosis. Genes Dev 2008; 22: 2707-2720.
    • (2008) Genes Dev , vol.22 , pp. 2707-2720
    • Archambault, V.1    D'Avino, P.P.2    Deery, M.J.3    Lilley, K.S.4    Glover, D.M.5
  • 54
    • 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, Nishida E. 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    Nishida, E.4
  • 55
    • 84860347756 scopus 로고    scopus 로고
    • Polo-like kinase-activating kinases: Aurora A Aurora B and what else
    • Archambault V, Carmena M. Polo-like kinase-activating kinases: Aurora A, Aurora B and what else? Cell Cycle 2012; 11: 1490-1495.
    • (2012) Cell Cycle , vol.11 , pp. 1490-1495
    • Archambault, V.1    Carmena, M.2
  • 56
  • 58
    • 0037113919 scopus 로고    scopus 로고
    • Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase
    • Jang YJ, Ma S, Terada Y, Erikson RL. Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase. J Biol Chem 2002; 277: 44115-44120.
    • (2002) J Biol Chem , vol.277 , pp. 44115-44120
    • Jang, Y.J.1    Ma, S.2    Terada, Y.3    Erikson, R.L.4
  • 59
    • 0033512308 scopus 로고    scopus 로고
    • Mitotic effects of a constitutively active mutant of the Xenopus polo-like kinase Plx1
    • Qian YW, Erikson E, Maller JL. Mitotic effects of a constitutively active mutant of the Xenopus polo-like kinase Plx1. Mol Cell Biol 1999; 19: 8625-8632.
    • (1999) Mol Cell Biol , vol.19 , pp. 8625-8632
    • Qian, Y.W.1    Erikson, E.2    Maller, J.L.3
  • 60
    • 51349144633 scopus 로고    scopus 로고
    • Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery
    • Macurek L, Lindqvist A, Lim D, Lampson MA, Klompmaker R, Freire R 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    Lampson, M.A.4    Klompmaker, R.5    Freire, R.6
  • 62
    • 84856508404 scopus 로고    scopus 로고
    • The chromosomal passenger complex activates Polo kinase at centromeres
    • Carmena M, Pinson X, Platani M, Salloum Z, Xu Z, Clark A et al. The chromosomal passenger complex activates Polo kinase at centromeres. PLoS Biol 2012; 10: e1001250.
    • (2012) PLoS Biol , vol.10 , pp. e1001250
    • Carmena, M.1    Pinson, X.2    Platani, M.3    Salloum, Z.4    Xu, Z.5    Clark, A.6
  • 63
    • 70549105789 scopus 로고    scopus 로고
    • Making the Auroras glow: Regulation of Aurora A and B kinase function by interacting proteins
    • Carmena M, Ruchaud S, Earnshaw WC. Making the Auroras glow: regulation of Aurora A and B kinase function by interacting proteins. Curr Opin Cell Biol 2009; 21: 796-805.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 796-805
    • Carmena, M.1    Ruchaud, S.2    Earnshaw, W.C.3
  • 64
    • 84870192369 scopus 로고    scopus 로고
    • The chromosomal passenger complex (CPC): From easy rider to the godfather of mitosis
    • Carmena M, Wheelock M, Funabiki H, Earnshaw WC. The chromosomal passenger complex (CPC): from easy rider to the godfather of mitosis. Nat Rev Mol Cell Biol 2012; 13: 789-803.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 789-803
    • Carmena, M.1    Wheelock, M.2    Funabiki, H.3    Earnshaw, W.C.4
  • 65
    • 84910672027 scopus 로고    scopus 로고
    • Interdomain allosteric regulation of Polo kinase by Aurora B and Map205 is required for cytokinesis
    • Kachaner D, Pinson X, El Kadhi KB, Normandin K, Talje L, Lavoie H et al. Interdomain allosteric regulation of Polo kinase by Aurora B and Map205 is required for cytokinesis. J Cell Biol 2014; 207: 201-211.
    • (2014) J Cell Biol , vol.207 , pp. 201-211
    • Kachaner, D.1    Pinson, X.2    El Kadhi, K.B.3    Normandin, K.4    Talje, L.5    Lavoie, H.6
  • 67
    • 65349102972 scopus 로고    scopus 로고
    • The decision to enter mitosis: Feedback and redundancy in the mitotic entry network
    • Lindqvist A, Rodriguez-Bravo V, Medema RH. The decision to enter mitosis: feedback and redundancy in the mitotic entry network. J Cell Biol 2009; 185: 193-202.
    • (2009) J Cell Biol , vol.185 , pp. 193-202
    • Lindqvist, A.1    Rodriguez-Bravo, V.2    Medema, R.H.3
  • 68
    • 14044263564 scopus 로고    scopus 로고
    • Uncoupling anaphase-promoting complex/cyclosome activity from spindle assembly checkpoint control by deregulating polo-like kinase 1
    • van de Weerdt BC, van Vugt MA, Lindon C, Kauw JJ, Rozendaal MJ, Klompmaker R et al. Uncoupling anaphase-promoting complex/cyclosome activity from spindle assembly checkpoint control by deregulating polo-like kinase 1. Mol Cell Biol 2005; 25: 2031-2044.
    • (2005) Mol Cell Biol , vol.25 , pp. 2031-2044
    • Van De Weerdt, B.C.1    Van Vugt, M.A.2    Lindon, C.3    Kauw, J.J.4    Rozendaal, M.J.5    Klompmaker, R.6
  • 69
    • 84878710374 scopus 로고    scopus 로고
    • PI 3-kinasedependent phosphorylation of Plk1-Ser99 promotes association with 14-3-3gamma and is required for metaphase-anaphase transition
    • Kasahara K, Goto H, Izawa I, Kiyono T, Watanabe N, Elowe S et al. PI 3-kinasedependent phosphorylation of Plk1-Ser99 promotes association with 14-3-3gamma and is required for metaphase-anaphase transition. Nat Commun 2013. 4-1882.
    • (2013) Nat Commun , pp. 4-1882
    • Kasahara, K.1    Goto, H.2    Izawa, I.3    Kiyono, T.4    Watanabe, N.5    Elowe, S.6
  • 70
    • 50049129364 scopus 로고    scopus 로고
    • P21-activated kinase is required for mitotic progression and regulates Plk1
    • Maroto B, Ye MB, von Lohneysen K, Schnelzer A, Knaus UG. P21-activated kinase is required for mitotic progression and regulates Plk1. Oncogene 2008; 27: 4900-4908.
    • (2008) Oncogene , vol.27 , pp. 4900-4908
    • Maroto, B.1    Ye, M.B.2    Von Lohneysen, K.3    Schnelzer, A.4    Knaus, U.G.5
  • 71
    • 43049101715 scopus 로고    scopus 로고
    • Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1
    • Yamashiro S, Yamakita Y, Totsukawa G, Goto H, Kaibuchi K, Ito M et al. Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1. Dev Cell 2008; 14: 787-797.
    • (2008) Dev Cell , vol.14 , pp. 787-797
    • Yamashiro, S.1    Yamakita, Y.2    Totsukawa, G.3    Goto, H.4    Kaibuchi, K.5    Ito, M.6
  • 72
    • 84872058611 scopus 로고    scopus 로고
    • A stringent requirement for Plk1 T210 phosphorylation during K-fiber assembly and chromosome congression
    • Paschal CR, Maciejowski J, Jallepalli PV. A stringent requirement for Plk1 T210 phosphorylation during K-fiber assembly and chromosome congression. Chromosoma 2012; 121: 565-572.
    • (2012) Chromosoma , vol.121 , pp. 565-572
    • Paschal, C.R.1    Maciejowski, J.2    Jallepalli, P.V.3
  • 73
    • 1642458099 scopus 로고    scopus 로고
    • Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells
    • Lindon C, Pines J. Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells. J Cell Biol 2004; 164: 233-241.
    • (2004) J Cell Biol , vol.164 , pp. 233-241
    • Lindon, C.1    Pines, J.2
  • 74
    • 84857437068 scopus 로고    scopus 로고
    • Plk1-dependent phosphorylation of optineurin provides a negative feedback mechanism for mitotic progression
    • Kachaner D, Filipe J, Laplantine E, Bauch A, Bennett KL, Superti-Furga G et al. Plk1-dependent phosphorylation of optineurin provides a negative feedback mechanism for mitotic progression. Mol Cell 2012; 45: 553-566.
    • (2012) Mol Cell , vol.45 , pp. 553-566
    • Kachaner, D.1    Filipe, J.2    Laplantine, E.3    Bauch, A.4    Bennett, K.L.5    Superti-Furga, G.6
  • 75
    • 84907743183 scopus 로고    scopus 로고
    • Centriole maturation requires regulated Plk1 activity during two consecutive cell cycles
    • Kong D, Farmer V, Shukla A, James J, Gruskin R, Kiriyama S et al. Centriole maturation requires regulated Plk1 activity during two consecutive cell cycles. J Cell Biol 2014; 206: 855-865.
    • (2014) J Cell Biol , vol.206 , pp. 855-865
    • Kong, D.1    Farmer, V.2    Shukla, A.3    James, J.4    Gruskin, R.5    Kiriyama, S.6
  • 76
    • 79953181967 scopus 로고    scopus 로고
    • Myosin phosphatase-targeting subunit 1 controls chromatid segregation
    • Matsumura F, Yamakita Y, Yamashiro S. Myosin phosphatase-targeting subunit 1 controls chromatid segregation. J Biol Chem 2011; 286: 10825-10833.
    • (2011) J Biol Chem , vol.286 , pp. 10825-10833
    • Matsumura, F.1    Yamakita, Y.2    Yamashiro, S.3
  • 77
    • 84890522100 scopus 로고    scopus 로고
    • Functions of the Hsp90 chaperone system: Lifting client proteins to new heights
    • Eckl JM, Richter K. Functions of the Hsp90 chaperone system: lifting client proteins to new heights. Int J Biochem Mol Biol 2014; 4: 157-165.
    • (2014) Int J Biochem Mol Biol , vol.4 , pp. 157-165
    • Eckl, J.M.1    Richter, K.2
  • 78
    • 3442890567 scopus 로고    scopus 로고
    • Heat shock protein 90 regulates the metaphase-anaphase transition in a polo-like kinase-dependent manner
    • de Carcer G. Heat shock protein 90 regulates the metaphase-anaphase transition in a polo-like kinase-dependent manner. Cancer Res 2004; 64: 5106-5112.
    • (2004) Cancer Res , vol.64 , pp. 5106-5112
    • De Carcer, G.1
  • 79
    • 0035355510 scopus 로고    scopus 로고
    • Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability
    • de Carcer G, do Carmo Avides M, Lallena MJ, Glover DM, Gonzalez C. Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability. EMBO J 2001; 20: 2878-2884.
    • (2001) EMBO J , vol.20 , pp. 2878-2884
    • De Carcer, G.1    Do Carmo Avides, M.2    Lallena, M.J.3    Glover, D.M.4    Gonzalez, C.5
  • 80
    • 59649124272 scopus 로고    scopus 로고
    • Sgt1, a co-chaperone of Hsp90 stabilizes Polo and is required for centrosome organization
    • Martins T, Maia AF, Steffensen S, Sunkel CE. Sgt1, a co-chaperone of Hsp90 stabilizes Polo and is required for centrosome organization. EMBO J 2009; 28: 234-247.
    • (2009) EMBO J , vol.28 , pp. 234-247
    • Martins, T.1    Maia, A.F.2    Steffensen, S.3    Sunkel, C.E.4
  • 81
    • 77952088459 scopus 로고    scopus 로고
    • An overview of Cdk1-controlled targets and processes
    • Enserink JM, Kolodner RD. An overview of Cdk1-controlled targets and processes. Cell Div 2010; 5: 11.
    • (2010) Cell Div , vol.5 , pp. 11
    • Enserink, J.M.1    Kolodner, R.D.2
  • 82
    • 23844525856 scopus 로고    scopus 로고
    • Cyclin-dependent kinase (CDK) phosphorylation destabilizes somatic Wee1 via multiple pathways
    • Watanabe N, Arai H, Iwasaki J, Shiina M, Ogata K, Hunter T et al. Cyclin-dependent kinase (CDK) phosphorylation destabilizes somatic Wee1 via multiple pathways. Proc Natl Acad Sci USA 2005; 102: 11663-11668.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11663-11668
    • Watanabe, N.1    Arai, H.2    Iwasaki, J.3    Shiina, M.4    Ogata, K.5    Hunter, T.6
  • 83
    • 33751070826 scopus 로고    scopus 로고
    • Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation
    • Kang YH, Park JE, Yu LR, Soung NK, Yun SM, Bang JK et al. Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation. Mol Cell 2006; 24: 409-422.
    • (2006) Mol Cell , vol.24 , pp. 409-422
    • Kang, Y.H.1    Park, J.E.2    Yu, L.R.3    Soung, N.K.4    Yun, S.M.5    Bang, J.K.6
  • 84
    • 33847680936 scopus 로고    scopus 로고
    • Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization
    • Garcia-Alvarez B, de Carcer G, Ibanez S, Bragado-Nilsson E, Montoya G. Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization. Proc Natl Acad Sci USA 2007; 104: 3107-3112.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 3107-3112
    • Garcia-Alvarez, B.1    De Carcer, G.2    Ibanez, S.3    Bragado-Nilsson, E.4    Montoya, G.5
  • 85
    • 0022443306 scopus 로고
    • A microtubule-associated protein in Drosophila melanogaster: Identification, characterization, and isolation of coding sequences
    • Goldstein LS, Laymon RA, McIntosh JR. A microtubule-associated protein in Drosophila melanogaster: identification, characterization, and isolation of coding sequences. J Cell Biol 1986; 102: 2076-2087.
    • (1986) J Cell Biol , vol.102 , pp. 2076-2087
    • Goldstein, L.S.1    Laymon, R.A.2    McIntosh, J.R.3
  • 86
    • 84860388896 scopus 로고    scopus 로고
    • Serendipitous alkylation of a Plk1 ligand uncovers a new binding channel
    • Liu F, Park JE, Qian WJ, Lim D, Graber M, Berg T et al. Serendipitous alkylation of a Plk1 ligand uncovers a new binding channel. Nat Chem Biol 2011; 7: 595-601.
    • (2011) Nat Chem Biol , vol.7 , pp. 595-601
    • Liu, F.1    Park, J.E.2    Qian, W.J.3    Lim, D.4    Graber, M.5    Berg, T.6
  • 87
    • 79954578345 scopus 로고    scopus 로고
    • From crystal packing to molecular recognition: Prediction and discovery of a binding site on the surface of polo-like kinase 1
    • Sledz P, Stubbs CJ, Lang S, Yang YQ, McKenzie GJ, Venkitaraman AR et al. From crystal packing to molecular recognition: prediction and discovery of a binding site on the surface of polo-like kinase 1. Angew Chem Int Ed Engl 2011; 50: 4003-4006.
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 4003-4006
    • Sledz, P.1    Stubbs, C.J.2    Lang, S.3    Yang, Y.Q.4    McKenzie, G.J.5    Venkitaraman, A.R.6
  • 88
    • 78650672088 scopus 로고    scopus 로고
    • Dbf4 regulates the Cdc5 Polo-like kinase through a distinct non-canonical binding interaction
    • Chen YC, Weinreich M. Dbf4 regulates the Cdc5 Polo-like kinase through a distinct non-canonical binding interaction. J Biol Chem 2010; 285: 41244-41254.
    • (2010) J Biol Chem , vol.285 , pp. 41244-41254
    • Chen, Y.C.1    Weinreich, M.2
  • 89
    • 0033947670 scopus 로고    scopus 로고
    • Cdc7p-Dbf4p becomes famous in the cell cycle
    • Sclafani RA. Cdc7p-Dbf4p becomes famous in the cell cycle. J Cell Sci 2000; 113: 2111-2117.
    • (2000) J Cell Sci , vol.113 , pp. 2111-2117
    • Sclafani, R.A.1
  • 90
    • 67149141853 scopus 로고    scopus 로고
    • Cdc7p-Dbf4p regulates mitotic exit by inhibiting Polo kinase
    • Miller CT, Gabrielse C, Chen YC, Weinreich M. Cdc7p-Dbf4p regulates mitotic exit by inhibiting Polo kinase. PLoS Genet 2009; 5: e1000498.
    • (2009) PLoS Genet , vol.5 , pp. e1000498
    • Miller, C.T.1    Gabrielse, C.2    Chen, Y.C.3    Weinreich, M.4
  • 91
    • 37349094837 scopus 로고    scopus 로고
    • The inhibition of Polo Kinase by matrimony maintains G2 arrest in the meiotic cell cycle
    • Xiang Y, Takeo S, Florens L, Hughes SE, Huo LJ, Gilliland WD et al. The inhibition of Polo Kinase by matrimony maintains G2 arrest in the meiotic cell cycle. PLoS Biol 2007; 5: e323.
    • (2007) PLoS Biol , vol.5 , pp. e323
    • Xiang, Y.1    Takeo, S.2    Florens, L.3    Hughes, S.E.4    Huo, L.J.5    Gilliland, W.D.6
  • 92
    • 42049112169 scopus 로고    scopus 로고
    • Matrimony ties Polo down: Can this kinase get free
    • Smith SK, Jaspersen SL, Hawley RS. Matrimony ties Polo down: can this kinase get free? Cell Cycle 2008; 7: 698-701.
    • (2008) Cell Cycle , vol.7 , pp. 698-701
    • Smith, S.K.1    Jaspersen, S.L.2    Hawley, R.S.3
  • 93
    • 84884581476 scopus 로고    scopus 로고
    • A meiosis-specific form of the APC/C promotes the oocyte-to-embryo transition by decreasing levels of the Polo kinase inhibitor matrimony
    • Whitfield ZJ, Chisholm J, Hawley RS, Orr-Weaver TL. A meiosis-specific form of the APC/C promotes the oocyte-to-embryo transition by decreasing levels of the Polo kinase inhibitor matrimony. PLoS Biol 2013; 11: e1001648.
    • (2013) PLoS Biol , vol.11 , pp. e1001648
    • Whitfield, Z.J.1    Chisholm, J.2    Hawley, R.S.3    Orr-Weaver, T.L.4
  • 94
    • 84875546271 scopus 로고    scopus 로고
    • Binding of Drosophila Polo kinase to its regulator Matrimony is noncanonical and involves two separate functional domains
    • Bonner AM, Hughes SE, Chisholm JA, Smith SK, Slaughter BD, Unruh JR et al. Binding of Drosophila Polo kinase to its regulator Matrimony is noncanonical and involves two separate functional domains. Proc Natl Acad Sci USA 2013; 110: E1222-E1231.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E1222-E1231
    • Bonner, A.M.1    Hughes, S.E.2    Chisholm, J.A.3    Smith, S.K.4    Slaughter, B.D.5    Unruh, J.R.6
  • 97
    • 19544370361 scopus 로고    scopus 로고
    • Polo kinase links the stress pathway to cell cycle control and tip growth in fission yeast
    • Petersen J, Hagan IM. Polo kinase links the stress pathway to cell cycle control and tip growth in fission yeast. Nature 2005; 435: 507-512.
    • (2005) Nature , vol.435 , pp. 507-512
    • Petersen, J.1    Hagan, I.M.2
  • 98
    • 84903184496 scopus 로고    scopus 로고
    • Current assessment of polo-like kinases as anti-tumor drug targets
    • Craig SN, Wyatt MD, McInnes C. Current assessment of polo-like kinases as anti-tumor drug targets. Expert Opin Drug Discov 2014; 9: 773-789.
    • (2014) Expert Opin Drug Discov , vol.9 , pp. 773-789
    • Craig, S.N.1    Wyatt, M.D.2    McInnes, C.3
  • 99
    • 66149091940 scopus 로고    scopus 로고
    • A genome-wide RNAi screen identifies multiple synthetic lethal interactions with the Ras oncogene
    • Luo J, Emanuele MJ, Li D, Creighton CJ, Schlabach MR, Westbrook TF et al. A genome-wide RNAi screen identifies multiple synthetic lethal interactions with the Ras oncogene. Cell 2009; 137: 835-848.
    • (2009) Cell , vol.137 , pp. 835-848
    • Luo, J.1    Emanuele, M.J.2    Li, D.3    Creighton, C.J.4    Schlabach, M.R.5    Westbrook, T.F.6
  • 100
    • 33644767315 scopus 로고    scopus 로고
    • Normal cells, but not cancer cells, survive severe Plk1 depletion
    • Liu X, Lei M, Erikson RL. Normal cells, but not cancer cells, survive severe Plk1 depletion. Mol Cell Biol 2006; 26: 2093-2108.
    • (2006) Mol Cell Biol , vol.26 , pp. 2093-2108
    • Liu, X.1    Lei, M.2    Erikson, R.L.3
  • 101
    • 70149106223 scopus 로고    scopus 로고
    • Polo-like kinase 1 is overexpressed in acute myeloid leukemia and its inhibition preferentially targets the proliferation of leukemic cells
    • Renner AG, Dos Santos C, Recher C, Bailly C, Creancier L, Kruczynski A et al. Polo-like kinase 1 is overexpressed in acute myeloid leukemia and its inhibition preferentially targets the proliferation of leukemic cells. Blood 2009; 114: 659-662.
    • (2009) Blood , vol.114 , pp. 659-662
    • Renner, A.G.1    Dos Santos, C.2    Recher, C.3    Bailly, C.4    Creancier, L.5    Kruczynski, A.6
  • 102
    • 65649105075 scopus 로고    scopus 로고
    • BI 6727, a Polo-like kinase inhibitor with improved pharmacokinetic profile and broad antitumor activity
    • Rudolph D, Steegmaier M, Hoffmann M, Grauert M, Baum A, Quant J et al. BI 6727, a Polo-like kinase inhibitor with improved pharmacokinetic profile and broad antitumor activity. Clin Cancer Res 2009; 15: 3094-3102.
    • (2009) Clin Cancer Res , vol.15 , pp. 3094-3102
    • Rudolph, D.1    Steegmaier, M.2    Hoffmann, M.3    Grauert, M.4    Baum, A.5    Quant, J.6
  • 103
    • 70149099357 scopus 로고    scopus 로고
    • Distinct concentration-dependent effects of the polo-like kinase 1-specific inhibitor GSK461364A, including differential effect on apoptosis
    • Gilmartin AG, Bleam MR, Richter MC, Erskine SG, Kruger RG, Madden L et al. Distinct concentration-dependent effects of the polo-like kinase 1-specific inhibitor GSK461364A, including differential effect on apoptosis. Cancer Res 2009; 69: 6969-6977.
    • (2009) Cancer Res , vol.69 , pp. 6969-6977
    • Gilmartin, A.G.1    Bleam, M.R.2    Richter, M.C.3    Erskine, S.G.4    Kruger, R.G.5    Madden, L.6
  • 105
    • 66249092744 scopus 로고    scopus 로고
    • Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation
    • Wolfe BA, Takaki T, Petronczki M, Glotzer M. Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation. PLoS Biol 2009; 7: e1000110.
    • (2009) PLoS Biol , vol.7 , pp. e1000110
    • Wolfe, B.A.1    Takaki, T.2    Petronczki, M.3    Glotzer, M.4
  • 106
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang J, Yang PL, Gray NS. Targeting cancer with small molecule kinase inhibitors. Nat Rev Cancer 2009; 9: 28-39.
    • (2009) Nat Rev Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 107
    • 33846933218 scopus 로고    scopus 로고
    • BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo
    • Steegmaier M, Hoffmann M, Baum A, Lenart P, Petronczki M, Krssak M et al. BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo. Curr Biol 2007; 17: 316-322.
    • (2007) Curr Biol , vol.17 , pp. 316-322
    • Steegmaier, M.1    Hoffmann, M.2    Baum, A.3    Lenart, P.4    Petronczki, M.5    Krssak, M.6
  • 109
    • 0037200029 scopus 로고    scopus 로고
    • A spindle checkpoint arrest and a cytokinesis failure by the dominant-negative polo-box domain of Plk1 in U-2 OS cells
    • Seong YS, Kamijo K, Lee JS, Fernandez E, Kuriyama R, Miki T et al. A spindle checkpoint arrest and a cytokinesis failure by the dominant-negative polo-box domain of Plk1 in U-2 OS cells. J Biol Chem 2002; 277: 32282-32293.
    • (2002) J Biol Chem , vol.277 , pp. 32282-32293
    • Seong, Y.S.1    Kamijo, K.2    Lee, J.S.3    Fernandez, E.4    Kuriyama, R.5    Miki, T.6
  • 110
    • 30044436805 scopus 로고    scopus 로고
    • Different Plk1 functions show distinct dependencies on Polo-Box domain-mediated targeting
    • Hanisch A, Wehner A, Nigg EA, Sillje HH. Different Plk1 functions show distinct dependencies on Polo-Box domain-mediated targeting. Mol Biol Cell 2006; 17: 448-459.
    • (2006) Mol Biol Cell , vol.17 , pp. 448-459
    • Hanisch, A.1    Wehner, A.2    Nigg, E.A.3    Sillje, H.H.4
  • 111
    • 84871161766 scopus 로고    scopus 로고
    • High mitotic activity of Polo-like kinase 1 is required for chromosome segregation and genomic integrity in human epithelial cells
    • Lera RF, Burkard ME. High mitotic activity of Polo-like kinase 1 is required for chromosome segregation and genomic integrity in human epithelial cells. J Biol Chem 2012; 287: 42812-42825.
    • (2012) J Biol Chem , vol.287 , pp. 42812-42825
    • Lera, R.F.1    Burkard, M.E.2
  • 112
    • 84886784260 scopus 로고    scopus 로고
    • Peptide-based inhibitors of Plk1 polo-box domain containing mono-anionic phosphothreonine esters and their pivaloyloxymethyl prodrugs
    • Qian WJ, Park JE, Lim D, Park SY, Lee KW, Yaffe MB et al. Peptide-based inhibitors of Plk1 polo-box domain containing mono-anionic phosphothreonine esters and their pivaloyloxymethyl prodrugs. Chem Biol 2013; 20: 1255-1264.
    • (2013) Chem Biol , vol.20 , pp. 1255-1264
    • Qian, W.J.1    Park, J.E.2    Lim, D.3    Park, S.Y.4    Lee, K.W.5    Yaffe, M.B.6
  • 113
    • 43149093993 scopus 로고    scopus 로고
    • Inhibition of polo-like kinase 1 by blocking polo-box domain-dependent protein-protein interactions
    • Reindl W, Yuan J, Kramer A, Strebhardt K, Berg T. Inhibition of polo-like kinase 1 by blocking polo-box domain-dependent protein-protein interactions. Chem Biol 2008; 15: 459-466.
    • (2008) Chem Biol , vol.15 , pp. 459-466
    • Reindl, W.1    Yuan, J.2    Kramer, A.3    Strebhardt, K.4    Berg, T.5
  • 114
    • 80053229630 scopus 로고    scopus 로고
    • Polo-box domain inhibitor poloxin activates the spindle assembly checkpoint and inhibits tumor growth in vivo
    • Yuan J, Sanhaji M, Kramer A, Reindl W, Hofmann M, Kreis NN et al. Polo-box domain inhibitor poloxin activates the spindle assembly checkpoint and inhibits tumor growth in vivo. Am J Pathol 2011; 179: 2091-2099.
    • (2011) Am J Pathol , vol.179 , pp. 2091-2099
    • Yuan, J.1    Sanhaji, M.2    Kramer, A.3    Reindl, W.4    Hofmann, M.5    Kreis, N.N.6
  • 115
    • 84874074839 scopus 로고    scopus 로고
    • Thymoquinone blocks pSer/pThr recognition by Plk1 Polo-box domain as a phosphate mimic
    • Yin Z, Song Y, Rehse PH. Thymoquinone blocks pSer/pThr recognition by Plk1 Polo-box domain as a phosphate mimic. ACS Chem Biol 2013; 8: 303-308.
    • (2013) ACS Chem Biol , vol.8 , pp. 303-308
    • Yin, Z.1    Song, Y.2    Rehse, P.H.3
  • 116
    • 59049093510 scopus 로고    scopus 로고
    • Deficiency in chromosome congression by the inhibition of Plk1 polo box domain-dependent recognition
    • Watanabe N, Sekine T, Takagi M, Iwasaki J, Imamoto N, Kawasaki H et al. Deficiency in chromosome congression by the inhibition of Plk1 polo box domain-dependent recognition. J Biol Chem 2009; 284: 2344-2353.
    • (2009) J Biol Chem , vol.284 , pp. 2344-2353
    • Watanabe, N.1    Sekine, T.2    Takagi, M.3    Iwasaki, J.4    Imamoto, N.5    Kawasaki, H.6
  • 117
    • 77956624673 scopus 로고    scopus 로고
    • Exploring potential binding modes of small drug-like molecules to the Polo-Box Domain of human Polo-like kinase 1
    • Liao C, Park JE, Bang JK, Nicklaus MC, Lee KS. Exploring potential binding modes of small drug-like molecules to the Polo-Box Domain of human Polo-like kinase 1. ACS Med Chem Lett 2010; 1: 110-114.
    • (2010) ACS Med Chem Lett , vol.1 , pp. 110-114
    • Liao, C.1    Park, J.E.2    Bang, J.K.3    Nicklaus, M.C.4    Lee, K.S.5
  • 118
    • 80055072364 scopus 로고    scopus 로고
    • Independent modulation of the kinase and polo-box activities of Cdc5 protein unravels unique roles in the maintenance of genome stability
    • Ratsima H, Ladouceur AM, Pascariu M, Sauve V, Salloum Z, Maddox PS et al. Independent modulation of the kinase and polo-box activities of Cdc5 protein unravels unique roles in the maintenance of genome stability. Proc Natl Acad Sci USA 2011; 108: E914-E923.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. E914-E923
    • Ratsima, H.1    Ladouceur, A.M.2    Pascariu, M.3    Sauve, V.4    Salloum, Z.5    Maddox, P.S.6
  • 119
    • 84864871913 scopus 로고    scopus 로고
    • Targeting subcellular localization through the polo-box domain: Non-ATP competitive inhibitors recapitulate a PLK1 phenotype
    • McInnes C, Estes K, Baxter M, Yang Z, Farag DB, Johnston P et al. Targeting subcellular localization through the polo-box domain: non-ATP competitive inhibitors recapitulate a PLK1 phenotype. Mol Cancer Ther 2012; 11: 1683-1692.
    • (2012) Mol Cancer Ther , vol.11 , pp. 1683-1692
    • McInnes, C.1    Estes, K.2    Baxter, M.3    Yang, Z.4    Farag, D.B.5    Johnston, P.6
  • 120
    • 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
  • 121
    • 80455160346 scopus 로고    scopus 로고
    • 14-3-3 proteins as signaling integration points for cell cycle control and apoptosis
    • Gardino AK, Yaffe MB. 14-3-3 proteins as signaling integration points for cell cycle control and apoptosis. Semin Cell Dev Biol 2011; 22: 688-695.
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 688-695
    • Gardino, A.K.1    Yaffe, M.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.