메뉴 건너뛰기




Volumn 14, Issue 7, 2009, Pages 775-788

Plk3 inhibits pro-apoptotic activity of p73 through physical interaction and phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

CISPLATIN; POLO LIKE KINASE 3; PROTEIN P73; SMALL INTERFERING RNA;

EID: 67649506339     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/j.1365-2443.2009.01309.x     Document Type: Article
Times cited : (13)

References (33)
  • 1
    • 4644221985 scopus 로고    scopus 로고
    • Murine FGF-inducible kinase is rapidly degraded via the nuclear ubiquitin-proteosome system when overexpressed in NIH 3T3 cells
    • Alberts, G.F. & Winkles, J.A. (2004) Murine FGF-inducible kinase is rapidly degraded via the nuclear ubiquitin-proteosome system when overexpressed in NIH 3T3 cells. Cell Cycle 3, 678-684.
    • (2004) Cell Cycle , vol.3 , pp. 678-684
    • Alberts, G.F.1    Winkles, J.A.2
  • 3
    • 0034671732 scopus 로고    scopus 로고
    • Incomplete cytokinesis and induction of apoptosis by overexpression of the mammalian polo-like kinase, Plk3
    • Conn, C.W., Hennigan, R.F., Dai, W., Sanchez, Y. & Stambrook, P.J. (2000) Incomplete cytokinesis and induction of apoptosis by overexpression of the mammalian polo-like kinase, Plk3. Cancer Res. 60, 6826-6831.
    • (2000) Cancer Res , vol.60 , pp. 6826-6831
    • Conn, C.W.1    Hennigan, R.F.2    Dai, W.3    Sanchez, Y.4    Stambrook, P.J.5
  • 4
    • 0028960192 scopus 로고
    • Identification by targeted differential display of an immediate early gene encoding a putative serine/threonine kinase
    • Donohue, P.J., Alberts, G.F., Guo, Y. & Winkles, J.A. (1995) Identification by targeted differential display of an immediate early gene encoding a putative serine/threonine kinase. J. Biol. Chem. 270, 10351-10357.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10351-10357
    • Donohue, P.J.1    Alberts, G.F.2    Guo, Y.3    Winkles, J.A.4
  • 5
    • 0037179845 scopus 로고    scopus 로고
    • Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein involved in stress response pathways
    • el Bahassi, M., Conn, C.W., Myer, D.L., Hennigan, R.F., McGowan, C.H., Sanchez, Y. & Stambrook, P.J. (2002) Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein involved in stress response pathways. Oncogene 21, 6633-6640.
    • (2002) Oncogene , vol.21 , pp. 6633-6640
    • el Bahassi, M.1    Conn, C.W.2    Myer, D.L.3    Hennigan, R.F.4    McGowan, C.H.5    Sanchez, Y.6    Stambrook, P.J.7
  • 6
    • 0242515843 scopus 로고    scopus 로고
    • Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates
    • Elia, A.E., Cantley, L.C. & Yaffe, M.B. (2003) Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates. Science 299, 1228-1231.
    • (2003) Science , vol.299 , pp. 1228-1231
    • Elia, A.E.1    Cantley, L.C.2    Yaffe, M.B.3
  • 7
    • 0035143449 scopus 로고    scopus 로고
    • Polo-like kinase interacts with proteasomes and regulates their activity
    • Feng, Y., Longo, D.L. & Ferris, D.K. (2001) Polo-like kinase interacts with proteasomes and regulates their activity. Cell Growth Differ. 12, 29-37.
    • (2001) Cell Growth Differ , vol.12 , pp. 29-37
    • Feng, Y.1    Longo, D.L.2    Ferris, D.K.3
  • 8
    • 0042347445 scopus 로고    scopus 로고
    • Cyclin-dependent kinases phosphorylate p73 at threonine 86 in a cell cycle-dependent manner and negatively regulate p73
    • Gaiddon, C., Lokshin, M., Gross, I., Levasseur, D., Taya, Y., Loeffler, J.-P. & Prives, C. (2003) Cyclin-dependent kinases phosphorylate p73 at threonine 86 in a cell cycle-dependent manner and negatively regulate p73. J. Biol. Chem. 278, 27421-27431.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27421-27431
    • Gaiddon, C.1    Lokshin, M.2    Gross, I.3    Levasseur, D.4    Taya, Y.5    Loeffler, J.-P.6    Prives, C.7
  • 9
    • 24044547036 scopus 로고    scopus 로고
    • Regulating the regulators: Control of protein ubiquitination and ubiquitin-like modifications by extracellular stimuli
    • Gao, M. & Karin, M. (2005) Regulating the regulators: Control of protein ubiquitination and ubiquitin-like modifications by extracellular stimuli. Mol. Cell 19, 581-593.
    • (2005) Mol. Cell , vol.19 , pp. 581-593
    • Gao, M.1    Karin, M.2
  • 10
    • 0033600234 scopus 로고    scopus 로고
    • The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage
    • Gong, J., Costanzo, A., Yang, H.-Q., Melino, G., Kaelin, W.G. Jr, Levreno, M. & Wang, J.Y. (1999) The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage. Nature 399, 806-809.
    • (1999) Nature , vol.399 , pp. 806-809
    • Gong, J.1    Costanzo, A.2    Yang, H.-Q.3    Melino, G.4    Kaelin, W.G.5    Levreno, M.6    Wang, J.Y.7
  • 11
    • 0242664079 scopus 로고    scopus 로고
    • p73α regulation by Chk1 in response to DNA damage
    • Gonzalez, S., Prives, C. & Cordon-Cordo, C. (2003) p73α regulation by Chk1 in response to DNA damage. Mol. Cell. Biol. 23, 8161-8171.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8161-8171
    • Gonzalez, S.1    Prives, C.2    Cordon-Cordo, C.3
  • 12
    • 33744520878 scopus 로고    scopus 로고
    • 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. (2006) Polo box domain of Plk3 functions as a centrosome localization signal, overexpression of which causes mitotic arrest, cytokinesis defects, and apoptosis. J. Biol. Chem. 281, 10577-10582.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10577-10582
    • Jiang, N.1    Wang, X.2    Jhanwar-Uniyal, M.3    Darzynkiewicz, Z.4    Dai, W.5
  • 13
    • 43749113592 scopus 로고    scopus 로고
    • Inhibitory role of Plk1 in the regulation of p73-dependent apoptosis through physical interaction and phosphorylation
    • Koida, N., Ozaki, T., Yamamoto, H., Ono, S., Koda, T., Ando, K., Okoshi, R., Kamijo, T., Omura, K. & Nakagawara, A. (2008) Inhibitory role of Plk1 in the regulation of p73-dependent apoptosis through physical interaction and phosphorylation. J. Biol. Chem. 283, 8555-8563.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8555-8563
    • Koida, N.1    Ozaki, T.2    Yamamoto, H.3    Ono, S.4    Koda, T.5    Ando, K.6    Okoshi, R.7    Kamijo, T.8    Omura, K.9    Nakagawara, A.10
  • 14
    • 0029770725 scopus 로고    scopus 로고
    • Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas
    • Li, B., Ouyang, B, Pan, H., Reissmann, P.T., Slamon, D.J., Arceci, R., Lu, L. & Dai, W. (1996) Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas. J. Biol. Chem. 271, 19402-19408.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19402-19408
    • Li, B.1    Ouyang, B.2    Pan, H.3    Reissmann, P.T.4    Slamon, D.J.5    Arceci, R.6    Lu, L.7    Dai, W.8
  • 15
    • 20444444295 scopus 로고    scopus 로고
    • Function of polo-like kinase 3 in NF-κB-mediated proapoptotic response
    • Li, Z., Niu, J., Uwagawa, T., Peng, B. & Chiao, P.J. (2005) Function of polo-like kinase 3 in NF-κB-mediated proapoptotic response. J. Biol. Chem. 280, 16843-16850.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16843-16850
    • Li, Z.1    Niu, J.2    Uwagawa, T.3    Peng, B.4    Chiao, P.J.5
  • 16
    • 41649094151 scopus 로고    scopus 로고
    • Plk3 phosphorylates topoisomerase IIa at Thr(1342), a site that is not recognized by Plk1
    • Iida, M., Matsuda, M. & Komatani, H. (2008) Plk3 phosphorylates topoisomerase IIa at Thr(1342), a site that is not recognized by Plk1. Biochem. J. 411, 27-32.
    • (2008) Biochem. J. , vol.411 , pp. 27-32
    • Iida, M.1    Matsuda, M.2    Komatani, H.3
  • 17
    • 34047276295 scopus 로고    scopus 로고
    • Polo-like kinases inhibited by wortmannin. Labeling site and downstream effects
    • Liu, Y., Jiang, N., Wu, J., Dai, W. & Rosenblum, J.S. (2007) Polo-like kinases inhibited by wortmannin. Labeling site and downstream effects. J. Biol. Chem. 282, 2505-2511.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2505-2511
    • Liu, Y.1    Jiang, N.2    Wu, J.3    Dai, W.4    Rosenblum, J.S.5
  • 18
    • 13244284602 scopus 로고    scopus 로고
    • Structure and function of Polo-like kinases
    • Lowery, D.M., Lim, D. & Yaffe, M.B. (2005) Structure and function of Polo-like kinases. Oncogene 24, 248-259.
    • (2005) Oncogene , vol.24 , pp. 248-259
    • Lowery, D.M.1    Lim, D.2    Yaffe, M.B.3
  • 20
    • 29644436953 scopus 로고    scopus 로고
    • p73, a sophisticated p53 family member in the cancer world
    • Ozaki, T. & Nakagawara, A. (2005) p73, a sophisticated p53 family member in the cancer world. Cancer Sci. 96, 729-737.
    • (2005) Cancer Sci , vol.96 , pp. 729-737
    • Ozaki, T.1    Nakagawara, A.2
  • 21
    • 0037072483 scopus 로고    scopus 로고
    • p73b is regulated by protein kinase Cd catalytic fragment generated in the apoptotic response to DNA damage
    • Ren, J., Datta, R., Shioya, H., Li, Y., Oki, E., Biedermann, V., Bharti, A. & Kufe, D. (2002) p73b is regulated by protein kinase Cd catalytic fragment generated in the apoptotic response to DNA damage. J. Biol. Chem. 277, 33758-33765.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33758-33765
    • Ren, J.1    Datta, R.2    Shioya, H.3    Li, Y.4    Oki, E.5    Biedermann, V.6    Bharti, A.7    Kufe, D.8
  • 23
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., Huibregtse, J.M., Vierstra, R.D. & Howley, P.M. (1993) The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 26
    • 7244240783 scopus 로고    scopus 로고
    • c-Jun regulates the stability and activity of the p53 homologue, p73
    • Toh, W.H., Siddique, M.M., Boominathan, L., Lin, K.W. & Sabapathy, K. (2004) c-Jun regulates the stability and activity of the p53 homologue, p73. J. Biol. Chem. 279, 44713-44722.
    • (2004) J. Biol. Chem. , vol.279 , pp. 44713-44722
    • Toh, W.H.1    Siddique, M.M.2    Boominathan, L.3    Lin, K.W.4    Sabapathy, K.5
  • 27
    • 36148950114 scopus 로고    scopus 로고
    • Stress-induced c-Jun activation mediated by Polo-like kinase 3 in corneal epithelial cells
    • Wang, L., Dai, W. & Lu, L. (2007) Stress-induced c-Jun activation mediated by Polo-like kinase 3 in corneal epithelial cells. J. Biol. Chem. 282, 32121-32127.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32121-32127
    • Wang, L.1    Dai, W.2    Lu, L.3
  • 28
    • 0036242249 scopus 로고    scopus 로고
    • Cell cycle arrest and apoptosis induced by human Polo-like kinase 3 is mediated through perturbation of microtubule integrity
    • Wang, Q., Suqing, X., Chen, J., Fukasawa, K., Naik, U., Traganos, F., Darzynkiewicz, Z., Jhanwar-Uniyal, M. & Dai, W. (2002) Cell cycle arrest and apoptosis induced by human Polo-like kinase 3 is mediated through perturbation of microtubule integrity. Mol. Cell. Biol. 22, 3450-3459.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3450-3459
    • Wang, Q.1    Suqing, X.2    Chen, J.3    Fukasawa, K.4    Naik, U.5    Traganos, F.6    Darzynkiewicz, Z.7    Jhanwar-Uniyal, M.8    Dai, W.9
  • 30
    • 0035168571 scopus 로고    scopus 로고
    • Intron/exon organization and polymorphisms of the PLK3/PRK gene in human lung carcinoma cell lines
    • Wiest, J., Clark, A.M. & Dai, W. (2001) Intron/exon organization and polymorphisms of the PLK3/PRK gene in human lung carcinoma cell lines. Genes Chromosomes Cancer 32, 384-389.
    • (2001) Genes Chromosomes Cancer , vol.32 , pp. 384-389
    • Wiest, J.1    Clark, A.M.2    Dai, W.3
  • 31
    • 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, J.P., Husain, I., Conn, C., Stambrook, P., Jhanwar-Uniyal, M. & Dai, W. (2001) Plk3 functionally links DNA damage to cell cycle arrest and apoptosis at least in part via the p53 pathway. J. Biol. Chem. 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    Stambrook, P.7    Jhanwar-Uniyal, M.8    Dai, W.9
  • 32
    • 49249127687 scopus 로고    scopus 로고
    • Polo-like kinase 3 functions as a tumor suppressor and is a negative regulator of hypoxia-inducible factor-1 alpha under hypoxic conditions
    • Yang, Y., Bai, J., Shen, R., Brown, S., Komissarova, E., Huang, Y., Jiang, N., Alberts, G.F., Costa, M., Lu, L., Winkles, J.A. & Dai, W. (2008) 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. 68, 4077-4085.
    • (2008) Cancer Res , vol.68 , pp. 4077-4085
    • Yang, Y.1    Bai, J.2    Shen, R.3    Brown, S.4    Komissarova, E.5    Huang, Y.6    Jiang, N.7    Alberts, G.F.8    Costa, M.9    Lu, L.10    Winkles, J.A.11    Dai, W.12
  • 33
    • 33846904706 scopus 로고    scopus 로고
    • Polo-like kinase 3 is required for entry into S phase
    • Zimmerman, W.C. & Erikson, R.L. (2007) Polo-like kinase 3 is required for entry into S phase. Proc. Natl. Acad. Sci. USA 104, 1847-1852.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1847-1852
    • Zimmerman, W.C.1    Erikson, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.