Current assessment of polo-like kinases as anti-tumor drug targets

Bibliography

• McInnes C, Wyatt MD. PLK1 as an oncology target: current status and future potential. Drug Discov Today 2011;16:619-25
   PubMed Web of Science ®Google Scholar
• Hansen DV, Loktev AV, Ban KH, Jackson PK. Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbetaTrCP-dependent destruction of the APC Inhibitor Emi1. Mol Biol Cell 2004;15:5623-34
   PubMed Web of Science ®Google Scholar
• Yamamoto Y, Matsuyama H, Kawauchi S, et al. Overexpression of polo-like kinase 1 (PLK1) and chromosomal instability in bladder cancer. Oncology 2006;70:231-7
   Google Scholar
• Cogswell JP, Brown CE, Bisi JE, Neill SD. Dominant-negative polo-like kinase 1 induces mitotic catastrophe independent of cdc25C function. Cell Growth Differ 2000;11:615-23
   PubMedGoogle Scholar
• Wolf G, Elez R, Doermer A, et al. Prognostic significance of polo-like kinase (PLK) expression in non-small cell lung cancer. Oncogene 1997;14:543-9
   PubMed Web of Science ®Google Scholar
• Yuan J, Hoerlin A, Hock B, et al. Polo-like kinase, a novel marker for cellular proliferation. Am J Pathol 1997;150:1165-72
   PubMed Web of Science ®Google Scholar
• Takahashi T, Sano B, Nagata T, et al. Polo-like kinase 1 (PLK1) is overexpressed in primary colorectal cancers. Cancer Sci 2003;94:148-52
   PubMed Web of Science ®Google Scholar
• Rodel F, Keppner S, Capalbo G, et al. Polo-like kinase 1 as predictive marker and therapeutic target for radiotherapy in rectal cancer. Am J Pathol 2010;177:918-29
   Google Scholar
• Lu LY, Wood JL, Minter-Dykhouse K, et al. Polo-like kinase 1 is essential for early embryonic development and tumor suppression. Mol Cell Biol 2008;28:6870-6
   PubMed Web of Science ®Google Scholar
• Raab M, Kappel S, Kramer A, et al. Toxicity modelling of Plk1-targeted therapies in genetically engineered mice and cultured primary mammalian cells. Nat Commun 2011;2:395
   PubMed Web of Science ®Google Scholar
• Burns TF, Fei P, Scata KA, et al. Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic catastrophe in paclitaxel (taxol)-exposed cells. Mol Cell Biol 2003;23:5556-71
   PubMed Web of Science ®Google Scholar
• Warnke S, Kemmler S, Hames RS, et al. Polo-like kinase-2 is required for centriole duplication in mammalian cells. Curr Biol 2004;14:1200-7
   PubMed Web of Science ®Google Scholar
• Matthew EM, Yen TJ, Dicker DT, et al. Replication stress, defective S-phase checkpoint and increased death in Plk2-deficient human cancer cells. Cell Cycle 2007;6:2571-8
   PubMed Web of Science ®Google Scholar
• Syed N, Smith P, Sullivan A, et al. Transcriptional silencing of Polo-like kinase 2 (SNK/PLK2) is a frequent event in B-cell malignancies. Blood 2006;107:250-6
   PubMed Web of Science ®Google Scholar
• Bergeron M, Motter R, Tanaka P, et al. In vivo modulation of polo-like kinases supports a key role for PLK2 in Ser129 alpha-synuclein phosphorylation in mouse brain. Neuroscience 2014;256:72-82
   PubMed Web of Science ®Google Scholar
• Ouyang B, Wang Y, Wei D. Caenorhabditis elegans contains structural homologs of human prk and plk. DNA Seq 1999;10:109-13
   PubMed Web of Science ®Google Scholar
• Wang Q, Xie S, Chen J, et al. Cell cycle arrest and apoptosis induced by human polo-like kinase 3 mediated through perturbation of microtubule integrity. Mol Cell Biol 2002;22:3450-9
   PubMed Web of Science ®Google Scholar
• El Bahassi M, Conn CW, Myer DL, et al. Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein involved in stress response pathways. Oncogene 2002;21:6633-40
   PubMed Web of Science ®Google Scholar
• Xie S, Wu H, Wang Q, 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;276:43305-12
   PubMed Web of Science ®Google Scholar
• Winkles JA, Alberts GF. Differential regulation of polo-like kinase 1, 2, 3, and 4 gene expression in mammalian cells and tissues. Oncogene 2005;24:260-6
   PubMed Web of Science ®Google Scholar
• Yang Y, Bai J, Shen R, et al. Polo-like kinase 3 functions as a tumor suppressor and is a negative regulator of hypoxia-inducible factor-1 alpha under hypoxic conditions. Cancer Res 2008;68:4077-85
   PubMed Web of Science ®Google Scholar
• Xu D, Yao Y, Jiang X, et al. Regulation of PTEN stability and activity by Plk3. J Biol Chem 2010;285:39935-42
   PubMed Web of Science ®Google Scholar
• Conn CW, Hennigan RF, Dai W, et al. Incomplete cytokinesis and induction of apoptosis by overexpression of the mammalian polo-like kinase, Plk3. Cancer Res 2000;60:6826-31
   PubMed Web of Science ®Google Scholar
• Bettencourt-Dias M, Rodrigues-Martins A, Carpenter L, et al. SAK/PLK4 is required for centriole duplication and flagella development. Curr Biol 2005;15:2199-207
   PubMed Web of Science ®Google Scholar
• Hatch EM, Kulukian A, Holland AJ, et al. Cep152 interacts with Plk4 and is required for centriole duplication. J Cell Biol 2010;191:721-9
   PubMed Web of Science ®Google Scholar
• Habedanck R, Stierhof YD, Wilkinson CJ, Nigg EA. The Polo kinase Plk4 functions in centriole duplication. Nat Cell Biol 2005;7:1140-6
   PubMed Web of Science ®Google Scholar
• Swallow CJ, Ko MA, Siddiqui NU, et al. Sak/Plk4 and mitotic fidelity. Oncogene 2005;24:306-12
   PubMed Web of Science ®Google Scholar
• Bonni S, Ganuelas ML, Petrinac S, Hudson JW. Human Plk4 phosphorylates Cdc25C. Cell Cycle 2008;7:545-7
   PubMed Web of Science ®Google Scholar
• Morettin A, Ward A, Nantais J, Hudson JW. Gene expression patterns in heterozygous Plk4 murine embryonic fibroblasts. BMC Genomics 2009;10:319
   PubMed Web of Science ®Google Scholar
• Macmillan JC, Hudson JW, Bull S, et al. Comparative expression of the mitotic regulators SAK and PLK in colorectal cancer. Ann Surg Oncol 2001;8:729-40
   PubMed Web of Science ®Google Scholar
• Mak TW. Targeting the cell cycle in cancer: TTK (MPS1) and PLK4 as novel mitotic targets. Book of Abstracts. AACR 103rd Annual Meeting; Chicago, IL; 2012
   Google Scholar
• Mason J, Wei S, Luo X, et al. Inhibition of Polo-like kinase 4 as an anti-cancer strategy. Book of Abstracts. AACR 102nd Annual Meeting; 2 – 6 April 2011; Orlando, FL
   Google Scholar
• Laufer R, Forrest B, Li SW, et al. The discovery of PLK4 inhibitors: (E)-3-((1H-Indazol-6-yl)methylene)indolin-2-ones as novel antiproliferative agents. J Med Chem 2013;56:6069-87
   PubMed Web of Science ®Google Scholar
• Andrysik Z, Bernstein WZ, Deng L, et al. The novel mouse Polo-like kinase 5 responds to DNA damage and localizes in the nucleolus. Nucleic Acids Res 2010;38:2931-43
   PubMed Web of Science ®Google Scholar
• de Carcer G, Manning G, Malumbres M. From Plk1 to Plk5: functional evolution of polo-like kinases. Cell Cycle 2011;10:2255-62
   PubMed Web of Science ®Google Scholar
• de Carcer G, Escobar B, Higuero AM, et al. Plk5, a polo box domain-only protein with specific roles in neuron differentiation and glioblastoma suppression. Mol Cell Biol 2011;31:1225-39
   PubMed Web of Science ®Google Scholar
• Spankuch-Schmitt B, Wolf G, Solbach C, et al. Downregulation of human polo-like kinase activity by antisense oligonucleotides induces growth inhibition in cancer cells. Oncogene 2002;21:3162-71
   PubMed Web of Science ®Google Scholar
• Spankuch B, Matthess Y, Knecht R, et al. Cancer inhibition in nude mice after systemic application of U6 promoter-driven short hairpin RNAs against PLK1. J Natl Cancer Inst 2004;96:862-72
   PubMed Web of Science ®Google Scholar
• 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;65:2698-704
   PubMed Web of Science ®Google Scholar
• Reagan-Shaw S, Ahmad N. Silencing of polo-like kinase (Plk) 1 via siRNA causes induction of apoptosis and impairment of mitosis machinery in human prostate cancer cells: implications for the treatment of prostate cancer. FASEB J 2005;19:611-13
   PubMed Web of Science ®Google Scholar
• Schmit TL, Zhong W, Setaluri V, et al. Targeted depletion of Polo-like kinase (Plk) 1 through lentiviral shRNA or a small-molecule inhibitor causes mitotic catastrophe and induction of apoptosis in human melanoma cells. J Invest Dermatol 2009;129:2843-53
   PubMed Web of Science ®Google Scholar
• Liu X, Erikson RL. Polo-like kinase (Plk)1 depletion induces apoptosis in cancer cells. Proc Natl Acad Sci USA 2003;100:5789-94
   PubMed Web of Science ®Google Scholar
• Liu X, Lei M, Erikson RL. Normal cells, but not cancer cells, survive severe Plk1 depletion. Mol Cell Biol 2006;26:2093-108
   PubMed Web of Science ®Google Scholar
• Steegmaier M, Hoffmann M, Baum A, et al. BI 2536, a potent and selective inhibitor of polo-like kinase 1, inhibits tumor growth in vivo. Curr Biol 2007;17:316-22
   PubMed Web of Science ®Google Scholar
• 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;17:304-15
   PubMed Web of Science ®Google Scholar
• Sebastian M, Reck M, Waller CF, et al. The efficacy and safety of BI 2536, a novel Plk-1 inhibitor, in patients with stage IIIB/IV non-small cell lung cancer who had relapsed after, or failed, chemotherapy: results from an open-label, randomized phase II clinical trial. J Thorac Oncol 2010;5:1060-7
   PubMed Web of Science ®Google Scholar
• Schoffski P, Blay JY, De Greve J, et al. Multicentric parallel phase II trial of the polo-like kinase 1 inhibitor BI 2536 in patients with advanced head and neck cancer, breast cancer, ovarian cancer, soft tissue sarcoma and melanoma. The first protocol of the European Organization for Research and Treatment of Cancer (EORTC) Network Of Core Institutes (NOCI). Eur J Cancer 2010;46:2206-15
   PubMed Web of Science ®Google Scholar
• Hofheinz RD, Al-Batran SE, Hochhaus A, et al. An open-label, phase I study of the polo-like kinase-1 inhibitor, BI 2536, in patients with advanced solid tumors. Clin Cancer Res 2010;16:4666-74
   PubMed Web of Science ®Google Scholar
• Mross K, Frost A, Steinbild S, et al. Phase I dose escalation and pharmacokinetic study of BI 2536, a novel Polo-like kinase 1 inhibitor, in patients with advanced solid tumors. J Clin Oncol 2008;26:5511-17
   PubMed Web of Science ®Google Scholar
• Rudolph D, Steegmaier M, Hoffmann M, et al. BI 6727, a Polo-like kinase inhibitor with improved pharmacokinetic profile and broad antitumor activity. Clin Cancer Res 2009;15:3094-102
   PubMed Web of Science ®Google Scholar
• Sanhaji M, Kreis NN, Zimmer B, et al. p53 is not directly relevant to the response of Polo-like kinase 1 inhibitors. Cell Cycle 2012;11:543-53
   PubMed Web of Science ®Google Scholar
• Maertens J, Lübbert M, Fiedler W, et al. Phase I/II study of volasertib (BI 6727), an intravenous Polo-like kinase (Plk) inhibitor, in patients with acute myeloid leukemia (AML): results from the randomized phase II part for volasertib in combination with low-dose cytarabine (LDAC) versus LDAC monotherapy in patients with previously untreated AML ineligible for intensive treatment. ASH Annual Meeting and Exposition; 8 – 11 December 2012; Atlanta, Georgia
   Google Scholar
• Stadler WM, Vaughn DJ, Sonpavde G, et al. An open-label, single-arm, phase 2 trial of the polo-like kinase inhibitor volasertib (BI 6727) in patients with locally advanced or metastatic urothelial cancer. Cancer 2014;120:976-82
   PubMed Web of Science ®Google Scholar
• Lansing TJ, McConnell RT, Duckett DR, et al. In vitro biological activity of a novel small-molecule inhibitor of polo-like kinase 1. Mol Cancer Ther 2007;6:450-9
   PubMed Web of Science ®Google Scholar
• 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;19:1694-7
   PubMed Web of Science ®Google Scholar
• Degenhardt Y, Greshock J, Laquerre S, et al. Sensitivity of cancer cells to Plk1 inhibitor GSK461364A is associated with loss of p53 function and chromosome instability. Mol Cancer Ther 2010;9:2079-89
   PubMed Web of Science ®Google Scholar
• Olmos D, Barker D, Sharma R, et al. Phase I study of GSK461364, a specific and competitive Polo-like kinase 1 inhibitor, in patients with advanced solid malignancies. Clin Cancer Res 2011;17:3420-30
   PubMed Web of Science ®Google Scholar
• Olmos D, Allred A, Sharma R, et al. Phase I first-in-human study of the polo-like kinase-1 selective inhibitor, GSK461364, in patients with advanced solid tumors. J Clin Oncol 2009;27:3536
   Google Scholar
• Hikichi Y, Honda K, Hikami K, et al. TAK-960, a novel, orally available, selective inhibitor of polo-like kinase 1, shows broad-spectrum preclinical antitumor activity in multiple dosing regimens. Mol Cancer Ther 2012;11:700-9
   PubMed Web of Science ®Google Scholar
• Nie Z, Feher V, Natala S, et al. Discovery of TAK-960: an orally available small molecule inhibitor of polo-like kinase 1 (PLK1). Bioorg Med Chem Lett 2013;23:3662-6
   PubMed Web of Science ®Google Scholar
• Santamaria A, Neef R, Eberspacher U, 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;18:4024-36
   PubMed Web of Science ®Google Scholar
• Elia AE, Cantley LC, Yaffe MB. Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates. Science 2003;299:1228-31
   PubMed Web of Science ®Google Scholar
• Elia AE, Rellos P, Haire LF, et al. The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain. Cell 2003;115:83-95
   PubMed Web of Science ®Google Scholar
• Garcia-Alvarez B, de Carcer G, Ibanez S, et al. Molecular and structural basis of polo-like kinase 1 substrate recognition: implications in centrosomal localization. Proc Natl Acad Sci USA 2007;104:3107-12
   PubMed Web of Science ®Google Scholar
• 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;16:876-82
   PubMed Web of Science ®Google Scholar
• Fink J, Sanders K, Rippl A, et al. Cell type – dependent effects of Polo-like kinase 1 inhibition compared with targeted polo box interference in cancer cell lines. Mol Cancer Ther 2007;6:3189-97
   PubMed Web of Science ®Google Scholar
• Yuan J, Kramer A, Eckerdt F, et al. Efficient internalization of the polo-box of polo-like kinase 1 fused to an Antennapedia peptide results in inhibition of cancer cell proliferation. Cancer Res 2002;62:4186-90
   PubMed Web of Science ®Google Scholar
• Reindl W, Yuan J, Kramer A, et al. Inhibition of polo-like kinase 1 by blocking polo-box domain-dependent protein-protein interactions. Chem Biol 2008;15:459-66
   PubMed Web of Science ®Google Scholar
• Yuan J, Sanhaji M, Kramer A, et al. Polo-box domain inhibitor poloxin activates the spindle assembly checkpoint and inhibits tumor growth in vivo. Am J Pathol 2011;179:2091-9
   PubMed Web of Science ®Google Scholar
• McInnes C, Estes K, Baxter M, et al. Targeting subcellular localization through the polo-box domain: non-ATP competitive inhibitors recapitulate a PLK1 phenotype. Mol Cancer Ther 2012;11:1683-92
   PubMed Web of Science ®Google Scholar
• Watanabe N, Sekine T, Takagi M, et al. Deficiency in chromosome congression by the inhibition of Plk1 polo box domain-dependent recognition. J Biol Chem 2009;284:2344-53
   PubMed Web of Science ®Google Scholar
• Liu F, Park JE, Qian WJ, et al. Serendipitous alkylation of a Plk1 ligand uncovers a new binding channel. Nat Chem Biol 2011;7:595-601
   PubMed Web of Science ®Google Scholar
• Kim SM, Yoon S, Choi N, et al. In vivo tumor imaging using polo-box domain of polo-like kinase 1 targeted peptide. Biomaterials 2012;33:6915-25
   PubMed Web of Science ®Google Scholar
• McInnes C. The REPLACE strategy for generating non-ATP competitive inhibitors of cell-cycle protein kinases. In: Mannhold R, editor. Protein-protein interactions in drug discovery, methods and principles in medicinal chemistry. Wiley-VCH, Weinheim, Germany; 2013. p. 291-304
   Google Scholar
• Liu S, Premnath PN, Bolger JK, et al. Optimization of non-ATP competitive CDK/cyclin groove inhibitors through REPLACE-mediated fragment assembly. J Med Chem 2013;56:1573-82
   PubMed Web of Science ®Google Scholar
• Andrews MJ, Kontopidis G, McInnes C, et al. REPLACE: a strategy for iterative design of cyclin-binding groove inhibitors. ChemBioChem 2006;7:1909-15
   PubMed Web of Science ®Google Scholar
• Burkard ME, Santamaria A, Jallepalli PV. Enabling and disabling polo-like kinase 1 inhibition through chemical genetics. ACS Chem Biol 2012;7:978-81
   PubMed Web of Science ®Google Scholar
• Bates S, Vousden KH. Mechanisms of p53-mediated apoptosis. Cell Mol Life Sci 1999;55:28-37
   PubMed Web of Science ®Google Scholar
• Ando K, Ozaki T, Yamamoto H, et al. Polo-like kinase 1 (Plk1) inhibits p53 function by physical interaction and phosphorylation. J Biol Chem 2004;279:25549-61
   PubMed Web of Science ®Google Scholar
• Chen J, Dai G, Wang YQ, et al. Polo-like kinase 1 regulates mitotic arrest after UV irradiation through dephosphorylation of p53 and inducing p53 degradation. FEBS Lett 2006;580:3624-30
   PubMed Web of Science ®Google Scholar
• Yang X, Li H, Zhou Z, et al. Plk1-mediated phosphorylation of Topors regulates p53 stability. J Biol Chem 2009;284:18588-92
   PubMed Web of Science ®Google Scholar
• Liu XS, Li H, Song B, Liu X. Polo-like kinase 1 phosphorylation of G2 and S-phase-expressed 1 protein is essential for p53 inactivation during G2 checkpoint recovery. EMBO Rep 2010;11:626-32
   PubMed Web of Science ®Google Scholar
• Schmit TL, Zhong W, Nihal M, Ahmad N. Polo-like kinase 1 (Plk1) in non-melanoma skin cancers. Cell Cycle 2009;8:2697-702
   PubMed Web of Science ®Google Scholar
• Kho PS, Wang Z, Zhuang L, et al. p53-regulated transcriptional program associated with genotoxic stress-induced apoptosis. J Biol Chem 2004;279:21183-92
   PubMed Web of Science ®Google Scholar
• McKenzie L, King S, Marcar L, et al. p53-dependent repression of polo-like kinase-1 (PLK1). Cell Cycle 2010;9:4200-12
   PubMed Web of Science ®Google Scholar
• Sanhaji M, Louwen F, Zimmer B, et al. Polo-like kinase 1 inhibitors, mitotic stress and the tumor suppressor p53. Cell Cycle 2013;12:1340-51
   PubMed Web of Science ®Google Scholar
• King SI, Purdie CA, Bray SE, et al. Immunohistochemical detection of Polo-like kinase-1 (PLK1) in primary breast cancer is associated with TP53 mutation and poor clinical outcom. Breast Cancer Res 2012;14:R40
   Google Scholar
• Sur S, Pagliarini R, Bunz F, et al. A panel of isogenic human cancer cells suggests a therapeutic approach for cancers with inactivated p53. Proc Natl Acad Sci USA 2009;106:3964-9
   PubMed Web of Science ®Google Scholar
• Song MS, Salmena L, Pandolfi PP. The functions and regulation of the PTEN tumour suppressor. Nat Rev Mol Cell Biol 2012;13:283-96
   PubMed Web of Science ®Google Scholar
• Song MS, Carracedo A, Salmena L, et al. Nuclear PTEN regulates the APC-CDH1 tumor-suppressive complex in a phosphatase-independent manner. Cell 2011;144:187-99
   PubMed Web of Science ®Google Scholar
• Shen WH, Balajee AS, Wang J, et al. Essential role for nuclear PTEN in maintaining chromosomal integrity. Cell 2007;128:157-70
   PubMed Web of Science ®Google Scholar
• Liu XS, Song B, Elzey BD, et al. Polo-like kinase 1 facilitates loss of Pten tumor suppressor-induced prostate cancer formation. J Biol Chem 2011;286:35795-800
   PubMed Web of Science ®Google Scholar
• Luo J, Emanuele MJ, Li D, et al. A genome-wide RNAi screen identifies multiple synthetic lethal interactions with the Ras oncogene. Cell 2009;137:835-48
   PubMed Web of Science ®Google Scholar