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Gene Review

PLK1  -  polo-like kinase 1

Homo sapiens

Synonyms: PLK, PLK-1, Polo-like kinase 1, STPK13, Serine/threonine-protein kinase 13, ...
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Disease relevance of PLK1

  • Our results suggest that the phosphorylation of HSF1 by PLK1 is an essential step for HSF1 nuclear translocation by heat stress [1].
  • Furthermore, this study suggests that PLK1 is a novel independent prognostic marker in ovarian carcinomas [2].
  • When PLK1 function was blocked through adenovirus delivery of a dominant-negative gene, we observed tumor-selective apoptosis in most tumor cell lines [3].
  • In this study, the expression of PLK1 and PLK3 was determined immunohistochemically in tissue specimen of normal ovaries (n=9), cystadenomas (n=17), borderline tumours (n=13) and ovarian carcinomas (n=77) [2].
  • In this study, expression of PLK1 and PLK3 was determined immunohistochemically in tissue specimens of 135 breast carcinomas, and expression was correlated with clinicopathological parameters and patient prognosis [4].

High impact information on PLK1


Chemical compound and disease context of PLK1


Biological context of PLK1

  • This interaction results in the phosphorylation of HSF1 on serine 419 by PLK1 [1].
  • Polo-like kinase 1 (PLK1) is an evolutionarily conserved serine/threonine kinase essential for cell mitosis [13].
  • Nuclear run-on assays and mRNA stability studies demonstrated that the effect of NO. on PLK1 expression was associated with decreased transcription without changes in transcript stability [13].
  • Reporter gene experiments showed that NO. decreased activity of the PLK1 proximal promoter, an effect that was blocked by p38 MAPK inhibitor [13].
  • RESULTS: PLK1 gene knockdown was associated with increased cyclin B expression, increased cdc2 activity (but not with the expression levels), accumulation of gastric cancer cells at G2/M, improper mitotic spindle formation, delayed chromosome separation and delayed or arrested cytokinesis [8].

Anatomical context of PLK1

  • Also, loss of PLK1 function has been shown to induce mitotic catastrophe in a HeLa cervical carcinoma cell line but not in normal Hs68 fibroblasts [3].
  • In some lines, dominant-negative PLK1 induced a mitotic catastrophe similar to that published in HeLa cells (K. E. Mundt et al., Biochem. Biophys Res. Commun., 239: 377-385, 1997) [3].
  • Mitotic phosphorylation of cdc25C and activation of cdk1 was blocked by dominant-negative PLK1 in human mammary epithelial cells as well as in the tumor lines regardless of whether they underwent mitotic catastrophe [3].
  • Transcriptional silencing of Polo-like kinase 2 (SNK/PLK2) is a frequent event in B-cell malignancies [14].
  • Another kinase implicated in regulating progression through mitosis is Plk1 (polo-like kinase 1), the human homologue of the Drosophila gene product "polo." By antibody microinjection we have found that Plk1 is required for the functional maturation of centrosomes and hence for entry into mitosis [15].

Associations of PLK1 with chemical compounds

  • Nitric oxide (NO.) has been shown to down-regulate PLK1 and up-regulate p21/Waf1 independent of cGMP [13].
  • Here, we show that treatment of mitotic cells with doxorubicin and gamma-irradiation inhibits Plk1 activity through dephosphorylation of Plk1, and cells were arrested in G(2) phase [16].
  • Nitric Oxide Down-regulates Polo-like Kinase 1 through a Proximal Promoter Cell Cycle Gene Homology Region [13].
  • These results suggest that suppression of the activity of PLK1 via inhibition of tyrosine kinase activity by beta-HIVS might play a critical role in the induction of apoptosis [17].
  • Here, we report that wortmannin, which was previously thought to be a highly selective inhibitor of phosphoinositide (PI) 3-kinases, is a potent inhibitor of mammalian PLK1 [18].
  • Kif2a is regulated positively by Plk1 and negatively by Aurora A [19].

Physical interactions of PLK1


Enzymatic interactions of PLK1


Regulatory relationships of PLK1


Co-localisations of PLK1

  • We go on to characterize the mitosis-specific interaction of the Plk1-PBD with the cytokinesis effector kinase Rho-associated coiled-coil domain-containing protein kinase 2 (Rock2), demonstrate that Rock2 is a Plk1 substrate, and show that Rock2 colocalizes with Plk1 during cytokinesis [33].

Other interactions of PLK1


Analytical, diagnostic and therapeutic context of PLK1


  1. Polo-like kinase 1 phosphorylates heat shock transcription factor 1 and mediates its nuclear translocation during heat stress. Kim, S.A., Yoon, J.H., Lee, S.H., Ahn, S.G. J. Biol. Chem. (2005) [Pubmed]
  2. Polo-like kinase isoform expression is a prognostic factor in ovarian carcinoma. Weichert, W., Denkert, C., Schmidt, M., Gekeler, V., Wolf, G., Köbel, M., Dietel, M., Hauptmann, S. Br. J. Cancer (2004) [Pubmed]
  3. Dominant-negative polo-like kinase 1 induces mitotic catastrophe independent of cdc25C function. Cogswell, J.P., Brown, C.E., Bisi, J.E., Neill, S.D. Cell Growth Differ. (2000) [Pubmed]
  4. Polo-like kinase isoforms in breast cancer: expression patterns and prognostic implications. Weichert, W., Kristiansen, G., Winzer, K.J., Schmidt, M., Gekeler, V., Noske, A., Müller, B.M., Niesporek, S., Dietel, M., Denkert, C. Virchows Arch. (2005) [Pubmed]
  5. PICH, a Centromere-Associated SNF2 Family ATPase, Is Regulated by Plk1 and Required for the Spindle Checkpoint. Baumann, C., K??rner, R., Hofmann, K., Nigg, E.A. Cell (2007) [Pubmed]
  6. The evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor emi1. Eldridge, A.G., Loktev, A.V., Hansen, D.V., Verschuren, E.W., Reimann, J.D., Jackson, P.K. Cell (2006) [Pubmed]
  7. Polo-like kinase 1 phosphorylates cyclin B1 and targets it to the nucleus during prophase. Toyoshima-Morimoto, F., Taniguchi, E., Shinya, N., Iwamatsu, A., Nishida, E. Nature (2001) [Pubmed]
  8. Inhibitory effect of Polo-like kinase 1 depletion on mitosis and apoptosis of gastric cancer cells. Chen, X.H., Lan, B., Qu, Y., Zhang, X.Q., Cai, Q., Liu, B.Y., Zhu, Z.G. World J. Gastroenterol. (2006) [Pubmed]
  9. Downregulation of human polo-like kinase activity by antisense oligonucleotides induces growth inhibition in cancer cells. Spänkuch-Schmitt, B., Wolf, G., Solbach, C., Loibl, S., Knecht, R., Stegmüller, M., von Minckwitz, G., Kaufmann, M., Strebhardt, K. Oncogene (2002) [Pubmed]
  10. Influence of chk1 and plk1 silencing on radiation- or cisplatin-induced cytotoxicity in human malignant cells. Gao, Q., Huang, X., Tang, D., Cao, Y., Chen, G., Lu, Y., Zhuang, L., Wang, S., Xu, G., Zhou, J., Ma, D. Apoptosis (2006) [Pubmed]
  11. Down-regulation of Polo-like kinase 1 elevates drug sensitivity of breast cancer cells in vitro and in vivo. Spänkuch, B., Heim, S., Kurunci-Csacsko, E., Lindenau, C., Yuan, J., Kaufmann, M., Strebhardt, K. Cancer Res. (2006) [Pubmed]
  12. Changes of pyridoxal kinase expression and activity in the gerbil hippocampus following transient forebrain ischemia. Hwang, I.K., Yoo, K.Y., Kim, D.S., Eum, W.S., Park, J.K., Park, J., Kwon, O.S., Kang, T.C., Choi, S.Y., Won, M.H. Neuroscience (2004) [Pubmed]
  13. Nitric Oxide Down-regulates Polo-like Kinase 1 through a Proximal Promoter Cell Cycle Gene Homology Region. Zhang, J., Wang, S., Kern, S., Cui, X., Danner, R.L. J. Biol. Chem. (2007) [Pubmed]
  14. Transcriptional silencing of Polo-like kinase 2 (SNK/PLK2) is a frequent event in B-cell malignancies. Syed, N., Smith, P., Sullivan, A., Spender, L.C., Dyer, M., Karran, L., O'Nions, J., Allday, M., Hoffmann, I., Crawford, D., Griffin, B., Farrell, P.J., Crook, T. Blood (2006) [Pubmed]
  15. Dynamic changes in nuclear architecture during mitosis: on the role of protein phosphorylation in spindle assembly and chromosome segregation. Nigg, E.A., Blangy, A., Lane, H.A. Exp. Cell Res. (1996) [Pubmed]
  16. Regulation of Polo-like Kinase 1 by DNA Damage in Mitosis: INHIBITION OF MITOTIC PLK-1 BY PROTEIN PHOSPHATASE 2A. Jang, Y.J., Ji, J.H., Choi, Y.C., Ryu, C.J., Ko, S.Y. J. Biol. Chem. (2007) [Pubmed]
  17. Beta-hydroxyisovalerylshikonin induces apoptosis in human leukemia cells by inhibiting the activity of a polo-like kinase 1 (PLK1). Masuda, Y., Nishida, A., Hori, K., Hirabayashi, T., Kajimoto, S., Nakajo, S., Kondo, T., Asaka, M., Nakaya, K. Oncogene (2003) [Pubmed]
  18. Wortmannin, a widely used phosphoinositide 3-kinase inhibitor, also potently inhibits mammalian polo-like kinase. Liu, Y., Shreder, K.R., Gai, W., Corral, S., Ferris, D.K., Rosenblum, J.S. Chem. Biol. (2005) [Pubmed]
  19. Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a. Jang, C.Y., Coppinger, J.A., Seki, A., Yates, J.R., Fang, G. J. Cell. Sci. (2009) [Pubmed]
  20. Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase stimulates association of the mitotic kinase Plk1 and accumulation of GTP-bound RhoA. Niiya, F., Tatsumoto, T., Lee, K.S., Miki, T. Oncogene (2006) [Pubmed]
  21. Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion. Litvak, V., Argov, R., Dahan, N., Ramachandran, S., Amarilio, R., Shainskaya, A., Lev, S. Mol. Cell (2004) [Pubmed]
  22. Interaction of chromatin-associated Plk1 and Mcm7. Tsvetkov, L., Stern, D.F. J. Biol. Chem. (2005) [Pubmed]
  23. Polo-like kinase 1 and Chk2 interact and co-localize to centrosomes and the midbody. Tsvetkov, L., Xu, X., Li, J., Stern, D.F. J. Biol. Chem. (2003) [Pubmed]
  24. SCFbetaTrCP-mediated degradation of Claspin regulates recovery from the DNA replication checkpoint response. Peschiaroli, A., Dorrello, N.V., Guardavaccaro, D., Venere, M., Halazonetis, T., Sherman, N.E., Pagano, M. Mol. Cell (2006) [Pubmed]
  25. 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. J. Biol. Chem. (2003) [Pubmed]
  26. The role of Polo-like kinase 1 in the inhibition of centrosome separation after ionizing radiation. Zhang, W., Fletcher, L., Muschel, R.J. J. Biol. Chem. (2005) [Pubmed]
  27. Phosphorylation of Plk1 at S137 and T210 is inhibited in response to DNA damage. Tsvetkov, L., Stern, D.F. Cell Cycle (2005) [Pubmed]
  28. Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbetaTrCP-dependent destruction of the APC Inhibitor Emi1. Hansen, D.V., Loktev, A.V., Ban, K.H., Jackson, P.K. Mol. Biol. Cell (2004) [Pubmed]
  29. Phosphorylation of BRCA2 by the Polo-like kinase Plk1 is regulated by DNA damage and mitotic progression. Lee, M., Daniels, M.J., Venkitaraman, A.R. Oncogene (2004) [Pubmed]
  30. Polo box domain of Plk3 functions as a centrosome localization signal, overexpression of which causes mitotic arrest, cytokinesis defects, and apoptosis. Jiang, N., Wang, X., Jhanwar-Uniyal, M., Darzynkiewicz, Z., Dai, W. J. Biol. Chem. (2006) [Pubmed]
  31. Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation. Kang, Y.H., Park, J.E., Yu, L.R., Soung, N.K., Yun, S.M., Bang, J.K., Seong, Y.S., Yu, H., Garfield, S., Veenstra, T.D., Lee, K.S. Mol. Cell (2006) [Pubmed]
  32. Regulation of I(kappa)B kinase complex by phosphorylation of (gamma)-binding domain of I(kappa)B kinase (beta) by Polo-like kinase 1. Higashimoto, T., Chan, N., Lee, Y.K., Zandi, E. J. Biol. Chem. (2008) [Pubmed]
  33. Proteomic screen defines the Polo-box domain interactome and identifies Rock2 as a Plk1 substrate. Lowery, D.M., Clauser, K.R., Hjerrild, M., Lim, D., Alexander, J., Kishi, K., Ong, S.E., Gammeltoft, S., Carr, S.A., Yaffe, M.B. EMBO J. (2007) [Pubmed]
  34. Mitotic regulation of the human anaphase-promoting complex by phosphorylation. Kraft, C., Herzog, F., Gieffers, C., Mechtler, K., Hagting, A., Pines, J., Peters, J.M. EMBO J. (2003) [Pubmed]
  35. 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., Hershko, A. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  36. Repression of mRNA for the PLK cell cycle gene after DNA damage requires BRCA1. Ree, A.H., Bratland, A., Nome, R.V., Stokke, T., Fodstad, Ø. Oncogene (2003) [Pubmed]
  37. Molecular interactions of Polo-like-kinase 1 with the mitotic kinesin-like protein CHO1/MKLP-1. Liu, X., Zhou, T., Kuriyama, R., Erikson, R.L. J. Cell. Sci. (2004) [Pubmed]
  38. 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, E.A., Sillje, H., Barr, F.A. Nat. Cell Biol. (2007) [Pubmed]
  39. Expression of polo-like kinase 1 (PLK1) protein predicts the survival of patients with gastric carcinoma. Kanaji, S., Saito, H., Tsujitani, S., Matsumoto, S., Tatebe, S., Kondo, A., Ozaki, M., Ito, H., Ikeguchi, M. Oncology (2006) [Pubmed]
  40. Polo-like kinase 1 expression is a prognostic factor in human colon cancer. Weichert, W., Kristiansen, G., Schmidt, M., Gekeler, V., Noske, A., Niesporek, S., Dietel, M., Denkert, C. World J. Gastroenterol. (2005) [Pubmed]
  41. B23/nucleophosmin serine 4 phosphorylation mediates mitotic functions of polo-like kinase 1. Zhang, H., Shi, X., Paddon, H., Hampong, M., Dai, W., Pelech, S. J. Biol. Chem. (2004) [Pubmed]
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