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Volumn 26, Issue 8, 2016, Pages 914-934

Ligand stimulation of CD95 induces activation of Plk3 followed by phosphorylation of caspase-8

Author keywords

apoptosis; caspase 8; CD95 Fas receptor; kinase regulation; polo like kinase

Indexed keywords

CASPASE 8; DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEIN; FADD PROTEIN, HUMAN; FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; LIGAND; PHOSPHOTHREONINE; PLK3 PROTEIN, HUMAN; PROTEIN BINDING; PROTEIN SERINE THREONINE KINASE;

EID: 84975263111     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2016.78     Document Type: Article
Times cited : (35)

References (69)
  • 1
    • 84870206960 scopus 로고    scopus 로고
    • Mitochondria: Master regulators of danger signalling
    • Galluzzi L, Kepp O, Kroemer G. Mitochondria: master regulators of danger signalling. Nat Rev Mol Cell Biol 2012; 13: 780-788.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 780-788
    • Galluzzi, L.1    Kepp, O.2    Kroemer, G.3
  • 2
    • 80054888589 scopus 로고    scopus 로고
    • It cuts both ways: Reconciling the dual roles of caspase 8 in cell death and survival
    • Oberst A, Green DR. It cuts both ways: reconciling the dual roles of caspase 8 in cell death and survival. Nat Rev Mol Cell Biol 2011; 12: 757-763.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 757-763
    • Oberst, A.1    Green, D.R.2
  • 3
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel FC, Hellbardt S, Behrmann I, et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J 1995; 14: 5579-5588.
    • (1995) EMBO J , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3
  • 4
    • 0035824635 scopus 로고    scopus 로고
    • Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8
    • Kischkel FC, Lawrence DA, Tinel A, et al. Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8. J Biol Chem 2001; 276: 46639-46646.
    • (2001) J Biol Chem , vol.276 , pp. 46639-46646
    • Kischkel, F.C.1    Lawrence, D.A.2    Tinel, A.3
  • 5
    • 0030925774 scopus 로고    scopus 로고
    • FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)
    • Medema JP, Scaffidi C, Kischkel FC, et al. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J 1997; 16: 2794-2804.
    • (1997) EMBO J , vol.16 , pp. 2794-2804
    • Medema, J.P.1    Scaffidi, C.2    Kischkel, F.C.3
  • 6
    • 0032536771 scopus 로고    scopus 로고
    • Two CD95 (APO-1/ Fas) signaling pathways
    • Scaffidi C, Fulda S, Srinivasan A, et al. Two CD95 (APO-1/ Fas) signaling pathways. EMBO J 1998; 17: 1675-1687.
    • (1998) EMBO J , vol.17 , pp. 1675-1687
    • Scaffidi, C.1    Fulda, S.2    Srinivasan, A.3
  • 8
    • 34247536682 scopus 로고    scopus 로고
    • The CD95 receptor: Apoptosis revisited
    • Peter ME, Budd RC, Desbarats J, et al. The CD95 receptor: apoptosis revisited. Cell 2007; 129: 447-450.
    • (2007) Cell , vol.129 , pp. 447-450
    • Peter, M.E.1    Budd, R.C.2    Desbarats, J.3
  • 9
    • 0024347970 scopus 로고
    • Monoclonal antibody-mediated tumor regression by induction of apoptosis
    • Trauth BC, Klas C, Peters AM, et al. Monoclonal antibody-mediated tumor regression by induction of apoptosis. Science 1989; 245: 301-305.
    • (1989) Science , vol.245 , pp. 301-305
    • Trauth, B.C.1    Klas, C.2    Peters, A.M.3
  • 10
    • 0027291205 scopus 로고
    • Lethal effect of the anti-Fas antibody in mice
    • Ogasawara J, Watanabe-Fukunaga R, Adachi M, et al. Lethal effect of the anti-Fas antibody in mice. Nature 1993; 364: 806-809.
    • (1993) Nature , vol.364 , pp. 806-809
    • Ogasawara, J.1    Watanabe-Fukunaga, R.2    Adachi, M.3
  • 12
    • 84930745615 scopus 로고    scopus 로고
    • Targeting Polo-like kinases: A promising therapeutic approach for cancer treatment
    • Liu X. Targeting Polo-like kinases: a promising therapeutic approach for cancer treatment. Transl Oncol 2015; 8: 185-195.
    • (2015) Transl Oncol , vol.8 , pp. 185-195
    • Liu, X.1
  • 13
    • 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
  • 14
    • 13244259198 scopus 로고    scopus 로고
    • Polo kinase and progression through M phase in Drosophila: A perspective from the spindle poles
    • Glover DM. Polo kinase and progression through M phase in Drosophila: a perspective from the spindle poles. Oncogene 2005; 24: 230-237.
    • (2005) Oncogene , vol.24 , pp. 230-237
    • Glover, D.M.1
  • 15
    • 13244255263 scopus 로고    scopus 로고
    • Yeast polo-like kinases: Functionally conserved multitask mitotic regulators
    • Lee KS, Park JE, Asano S, Park CJ. Yeast polo-like kinases: functionally conserved multitask mitotic regulators. Oncogene 2005; 24: 217-229.
    • (2005) Oncogene , vol.24 , pp. 217-229
    • Lee, K.S.1    Park, J.E.2    Asano, S.3    Park, C.J.4
  • 16
    • 13244269808 scopus 로고    scopus 로고
    • Polo-like kinases and oncogenesis
    • Eckerdt F, Yuan J, Strebhardt K. Polo-like kinases and oncogenesis. Oncogene 2005; 24: 267-276.
    • (2005) Oncogene , vol.24 , pp. 267-276
    • Eckerdt, F.1    Yuan, J.2    Strebhardt, K.3
  • 17
    • 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
  • 18
    • 0028348704 scopus 로고
    • Induction and down-regulation of PLK, a human serine/threonine kinase expressed in proliferating cells and tumors
    • Holtrich U, Wolf G, Brauninger A, et al. Induction and down-regulation of PLK, a human serine/threonine kinase expressed in proliferating cells and tumors. Proc Natl Acad Sci USA 1994; 91: 1736-1740.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1736-1740
    • Holtrich, U.1    Wolf, G.2    Brauninger, A.3
  • 19
    • 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
  • 20
    • 79960580428 scopus 로고    scopus 로고
    • Toxicity modelling of Plk1-targeted therapies in genetically engineered mice and cultured primary mammalian cells
    • 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.
    • (2011) Nat Commun , vol.2 , pp. 395
    • Raab, M.1    Kappel, S.2    Kramer, A.3
  • 21
    • 84887229523 scopus 로고    scopus 로고
    • Plk1: Unexpected roles in DNA replication
    • Mandal R, Strebhardt K. Plk1: unexpected roles in DNA replication. Cell Res 2013; 23: 1251-1253.
    • (2013) Cell Res , vol.23 , pp. 1251-1253
    • Mandal, R.1    Strebhardt, K.2
  • 22
    • 33845624084 scopus 로고    scopus 로고
    • Polo-like kinase 1: Target and regulator of transcriptional control
    • Martin BT, Strebhardt K. Polo-like kinase 1: target and regulator of transcriptional control. Cell Cycle 2006; 5: 2881-2885.
    • (2006) Cell Cycle , vol.5 , pp. 2881-2885
    • Martin, B.T.1    Strebhardt, K.2
  • 23
    • 0036682358 scopus 로고    scopus 로고
    • Efficient internalization of the polo-box of polo-like kinase 1 fused to an Antennapedia peptide results in inhibition of cancer cell proliferation
    • Yuan J, Kramer A, Eckerdt F, Kaufmann M, Strebhardt K. 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: 4186-4190.
    • (2002) Cancer Res , vol.62 , pp. 4186-4190
    • Yuan, J.1    Kramer, A.2    Eckerdt, F.3    Kaufmann, M.4    Strebhardt, K.5
  • 24
    • 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, et al. Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas. J Biol Chem 1996; 271: 19402-19408.
    • (1996) J Biol Chem , vol.271 , pp. 19402-19408
    • Li, B.1    Ouyang, B.2    Pan, H.3
  • 25
    • 0034609729 scopus 로고    scopus 로고
    • Adhesion induced expression of the serine/threonine kinase Fnk in human macrophages
    • Holtrich U, Wolf G, Yuan J, et al. Adhesion induced expression of the serine/threonine kinase Fnk in human macrophages. Oncogene 2000; 19: 4832-4839.
    • (2000) Oncogene , vol.19 , pp. 4832-4839
    • Holtrich, U.1    Wolf, G.2    Yuan, J.3
  • 26
    • 17144458001 scopus 로고    scopus 로고
    • PRK, a cell cycle gene localized to 8p21, is downregulated in head and neck cancer
    • Dai W, Li Y, Ouyang B, et al. PRK, a cell cycle gene localized to 8p21, is downregulated in head and neck cancer. Genes Chromosomes Cancer 2000; 27: 332-336.
    • (2000) Genes Chromosomes Cancer , vol.27 , pp. 332-336
    • Dai, W.1    Li, Y.2    Ouyang, B.3
  • 28
    • 77955525117 scopus 로고    scopus 로고
    • RNAi screening of the kinome identifies modulators of cisplatin response in ovarian cancer cells
    • Arora S, Bisanz KM, Peralta LA, et al. RNAi screening of the kinome identifies modulators of cisplatin response in ovarian cancer cells. Gynecol Oncol 2010; 118: 220-227.
    • (2010) Gynecol Oncol , vol.118 , pp. 220-227
    • Arora, S.1    Bisanz, K.M.2    Peralta, L.A.3
  • 29
    • 0037276437 scopus 로고    scopus 로고
    • The CD95(APO-1/Fas) DISC and beyond
    • Peter ME, Krammer PH. The CD95(APO-1/Fas) DISC and beyond. Cell Death Differ 2003; 10: 26-35.
    • (2003) Cell Death Differ , vol.10 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 30
    • 84912106351 scopus 로고    scopus 로고
    • RIP3 induces apoptosis independent of pronecrotic kinase activity
    • Mandal P, Berger SB, Pillay S, et al. RIP3 induces apoptosis independent of pronecrotic kinase activity. Mol Cell 2014; 56: 481-495.
    • (2014) Mol Cell , vol.56 , pp. 481-495
    • Mandal, P.1    Berger, S.B.2    Pillay, S.3
  • 31
    • 79960297569 scopus 로고    scopus 로고
    • Cdk1/cyclin B1 controls Fas-mediated apoptosis by regulating caspase-8 activity
    • Matthess Y, Raab M, Sanhaji M, Lavrik IN, Strebhardt K. Cdk1/cyclin B1 controls Fas-mediated apoptosis by regulating caspase-8 activity. Mol Cell Biol 2010; 30: 5726-5740.
    • (2010) Mol Cell Biol , vol.30 , pp. 5726-5740
    • Matthess, Y.1    Raab, M.2    Sanhaji, M.3    Lavrik, I.N.4    Strebhardt, K.5
  • 32
    • 84899139994 scopus 로고    scopus 로고
    • Sequential Cdk1 and Plk1 phosphorylation of caspase-8 triggers apoptotic cell death during mitosis
    • Matthess Y, Raab M, Knecht R, Becker S, Strebhardt K. Sequential Cdk1 and Plk1 phosphorylation of caspase-8 triggers apoptotic cell death during mitosis. Mol Oncol 2014.
    • (2014) Mol Oncol
    • Matthess, Y.1    Raab, M.2    Knecht, R.3    Becker, S.4    Strebhardt, K.5
  • 33
    • 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. Polo box domain of Plk3 functions as a centrosome localization signal, overexpression of which causes mitotic arrest, cytokinesis defects, and apoptosis. J Biol Chem 2006; 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
  • 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, 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
  • 36
    • 78651277460 scopus 로고    scopus 로고
    • PHOSIDA 2011: The posttranslational modification database
    • Database issue
    • Gnad F, Gunawardena J, Mann M. PHOSIDA 2011: the posttranslational modification database. Nucleic Acids Res 2011; 39(Database issue): D253-D260.
    • (2011) Nucleic Acids Res , vol.39 , pp. D253-D260
    • Gnad, F.1    Gunawardena, J.2    Mann, M.3
  • 37
    • 78449310037 scopus 로고    scopus 로고
    • mRNA turnover rate limits siRNA and microRNA efficacy
    • Larsson E, Sander C, Marks D. mRNA turnover rate limits siRNA and microRNA efficacy. Mol Syst Biol 2010; 6: 433.
    • (2010) Mol Syst Biol , vol.6 , pp. 433
    • Larsson, E.1    Sander, C.2    Marks, D.3
  • 38
    • 33645316142 scopus 로고    scopus 로고
    • Targeting polo-like kinase 1 for cancer therapy
    • Strebhardt K, Ullrich A. Targeting polo-like kinase 1 for cancer therapy. Nat Rev Cancer 2006; 6: 321-330.
    • (2006) Nat Rev Cancer , vol.6 , pp. 321-330
    • Strebhardt, K.1    Ullrich, A.2
  • 39
    • 85027940580 scopus 로고    scopus 로고
    • Quantitative chemical proteomics reveals a Plk1 inhibitor-compromised cell death pathway in human cells
    • Raab M, Pachl F, Kramer A, et al. Quantitative chemical proteomics reveals a Plk1 inhibitor-compromised cell death pathway in human cells. Cell Res 2014; 24: 1141-1145.
    • (2014) Cell Res , vol.24 , pp. 1141-1145
    • Raab, M.1    Pachl, F.2    Kramer, A.3
  • 40
    • 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
  • 41
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of Mach, a novel MORT1/FADD-interacting protease, in Fas/APO-1-and TNF receptor-induced cell death
    • Boldin MP, Goncharov TM, Goltsev YV, Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1-and TNF receptor-induced cell death. Cell 1996; 85: 803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 42
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio M, Chinnaiyan AM, Kischkel FC, et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 1996; 85: 817-827.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3
  • 43
    • 84922132326 scopus 로고    scopus 로고
    • Tumor-specific cytotoxic T lymphocyte activity determines colorectal cancer patient prognosis
    • Reissfelder C, Stamova S, Gossmann C, et al. Tumor-specific cytotoxic T lymphocyte activity determines colorectal cancer patient prognosis. J Clin Invest 2015; 125: 739-751.
    • (2015) J Clin Invest , vol.125 , pp. 739-751
    • Reissfelder, C.1    Stamova, S.2    Gossmann, C.3
  • 45
    • 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, Xie S, Chen J, et al. Cell cycle arrest and apoptosis induced by human Polo-like kinase 3 is mediated through perturbation of microtubule integrity. Mol Cell Biol 2002; 22: 3450-3459.
    • (2002) Mol Cell Biol , vol.22 , pp. 3450-3459
    • Wang, Q.1    Xie, S.2    Chen, J.3
  • 46
    • 0034671732 scopus 로고    scopus 로고
    • Incomplete cytokinesis and induction of apoptosis by overexpression of the mammalian polo-like kinase, Plk3
    • Conn CW, Hennigan RF, Dai W, Sanchez Y, Stambrook PJ. Incomplete cytokinesis and induction of apoptosis by overexpression of the mammalian polo-like kinase, Plk3. Cancer Res 2000; 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
  • 47
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 2010; 141: 1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 48
    • 0032488045 scopus 로고    scopus 로고
    • Lymphocyte signaling: Adapting new adaptors
    • Rudd CE. Lymphocyte signaling: adapting new adaptors. Curr Biol 1998; 8: R805-808.
    • (1998) Curr Biol , vol.8 , pp. R805-808
    • Rudd, C.E.1
  • 49
    • 40149099894 scopus 로고    scopus 로고
    • Yes and PI3K bind CD95 to signal invasion of glioblastoma
    • Kleber S, Sancho-Martinez I, Wiestler B, et al. Yes and PI3K bind CD95 to signal invasion of glioblastoma. Cancer Cell 2008; 13: 235-248.
    • (2008) Cancer Cell , vol.13 , pp. 235-248
    • Kleber, S.1    Sancho-Martinez, I.2    Wiestler, B.3
  • 50
    • 0033393957 scopus 로고    scopus 로고
    • TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src
    • Wong BR, Besser D, Kim N, et al. TRANCE, a TNF family member, activates Akt/PKB through a signaling complex involving TRAF6 and c-Src. Mol Cell 1999; 4: 1041-1049.
    • (1999) Mol Cell , vol.4 , pp. 1041-1049
    • Wong, B.R.1    Besser, D.2    Kim, N.3
  • 52
    • 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
  • 53
    • 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, 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
  • 54
    • 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
  • 55
    • 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
  • 56
    • 84894305596 scopus 로고    scopus 로고
    • PERK 1/2 inhibit Caspase-8 induced apoptosis in cancer cells by phosphorylating it in a cell cycle specific manner
    • Mandal R, Raab M, Matthess Y, Becker S, Knecht R, Strebhardt K. pERK 1/2 inhibit Caspase-8 induced apoptosis in cancer cells by phosphorylating it in a cell cycle specific manner. Mol Oncol 2014; 8: 232-249.
    • (2014) Mol Oncol , vol.8 , pp. 232-249
    • Mandal, R.1    Raab, M.2    Matthess, Y.3    Becker, S.4    Knecht, R.5    Strebhardt, K.6
  • 57
    • 33646542701 scopus 로고    scopus 로고
    • Src kinase phosphorylates Caspase-8 on Tyr380: A novel mechanism of apoptosis suppression
    • Cursi S, Rufini A, Stagni V, et al. Src kinase phosphorylates Caspase-8 on Tyr380: a novel mechanism of apoptosis suppression. EMBO J 2006; 25: 1895-1905.
    • (2006) EMBO J , vol.25 , pp. 1895-1905
    • Cursi, S.1    Rufini, A.2    Stagni, V.3
  • 59
    • 33645148675 scopus 로고    scopus 로고
    • Regulation of ubiquitin-binding proteins by monoubiquitination
    • Hoeller D, Crosetto N, Blagoev B, et al. Regulation of ubiquitin-binding proteins by monoubiquitination. Nat Cell Biol 2006; 8: 163-169.
    • (2006) Nat Cell Biol , vol.8 , pp. 163-169
    • Hoeller, D.1    Crosetto, N.2    Blagoev, B.3
  • 60
    • 0031578244 scopus 로고    scopus 로고
    • Malignant transformation of mammalian cells initiated by constitutive expression of the polo-like kinase
    • Smith MR, Wilson ML, Hamanaka R, et al. Malignant transformation of mammalian cells initiated by constitutive expression of the polo-like kinase. Biochem Biophys Res Commun 1997; 234: 397-405.
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 397-405
    • Smith, M.R.1    Wilson, M.L.2    Hamanaka, R.3
  • 61
    • 84954382715 scopus 로고    scopus 로고
    • The role of Plk3 in oncogenesis
    • Helmke C, Becker S, Strebhardt K. The role of Plk3 in oncogenesis. Oncogene 2016; 35: 135-147.
    • (2016) Oncogene , vol.35 , pp. 135-147
    • Helmke, C.1    Becker, S.2    Strebhardt, K.3
  • 62
    • 84942295891 scopus 로고    scopus 로고
    • Tumor-infiltrating CD8+ T lymphocytes associated with clinical outcome in anal squamous cell carcinoma
    • Hu WH, Miyai K, Cajas-Monson LC, Luo L, Liu L, Ramamoorthy SL. Tumor-infiltrating CD8+ T lymphocytes associated with clinical outcome in anal squamous cell carcinoma. J Surg Oncol 2015; 112: 421-426.
    • (2015) J Surg Oncol , vol.112 , pp. 421-426
    • Hu, W.H.1    Miyai, K.2    Cajas-Monson, L.C.3    Luo, L.4    Liu, L.5    Ramamoorthy, S.L.6
  • 63
    • 33645033152 scopus 로고    scopus 로고
    • Stable gene silencing of cyclin B1 in tumor cells increases susceptibility to taxol and leads to growth arrest in vivo
    • Yuan J, Kramer A, Matthess Y, et al. Stable gene silencing of cyclin B1 in tumor cells increases susceptibility to taxol and leads to growth arrest in vivo. Oncogene 2006; 25: 1753-1762.
    • (2006) Oncogene , vol.25 , pp. 1753-1762
    • Yuan, J.1    Kramer, A.2    Matthess, Y.3
  • 64
    • 18744364690 scopus 로고    scopus 로고
    • Apoptotic rate: A new indicator for the quantification of the incidence of apoptosis in cell cultures
    • Prieto A, Diaz D, Barcenilla H, et al. Apoptotic rate: a new indicator for the quantification of the incidence of apoptosis in cell cultures. Cytometry 2002; 48: 185-193.
    • (2002) Cytometry , vol.48 , pp. 185-193
    • Prieto, A.1    Diaz, D.2    Barcenilla, H.3
  • 65
    • 70350416297 scopus 로고    scopus 로고
    • SLP-65 phosphorylation dynamics reveals a functional basis for signal integration by receptor-proximal adaptor proteins
    • Oellerich T, Gronborg M, Neumann K, Hsiao HH, Urlaub H, Wienands J. SLP-65 phosphorylation dynamics reveals a functional basis for signal integration by receptor-proximal adaptor proteins. Mol Cell Proteomics 2009; 8: 1738-1750.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1738-1750
    • Oellerich, T.1    Gronborg, M.2    Neumann, K.3    Hsiao, H.H.4    Urlaub, H.5    Wienands, J.6
  • 66
    • 84901773291 scopus 로고    scopus 로고
    • PADI4 acts as a coactivator of Tal1 by counteracting repressive histone arginine methylation
    • Kolodziej S, Kuvardina ON, Oellerich T, et al. PADI4 acts as a coactivator of Tal1 by counteracting repressive histone arginine methylation. Nat Commun 2014; 5: 3995.
    • (2014) Nat Commun , vol.5 , pp. 3995
    • Kolodziej, S.1    Kuvardina, O.N.2    Oellerich, T.3
  • 67
    • 84922311673 scopus 로고    scopus 로고
    • Human papillomavirus DNA load and p16INK4a expression predict for local control in patients with anal squamous cell carcinoma treated with chemoradiotherapy
    • Rodel F, Wieland U, Fraunholz I, et al. Human papillomavirus DNA load and p16INK4a expression predict for local control in patients with anal squamous cell carcinoma treated with chemoradiotherapy. Int J Cancer 2015; 136: 278-288.
    • (2015) Int J Cancer , vol.136 , pp. 278-288
    • Rodel, F.1    Wieland, U.2    Fraunholz, I.3
  • 68
    • 0037132736 scopus 로고    scopus 로고
    • Effect of RNA silencing of polo-like kinase-1 (PLK1) on apoptosis and spindle formation in human cancer cells
    • Spankuch-Schmitt B, Bereiter-Hahn J, Kaufmann M, Strebhardt K. Effect of RNA silencing of polo-like kinase-1 (PLK1) on apoptosis and spindle formation in human cancer cells. J Natl Cancer Inst 2002; 94: 1863-1877.
    • (2002) J Natl Cancer Inst , vol.94 , pp. 1863-1877
    • Spankuch-Schmitt, B.1    Bereiter-Hahn, J.2    Kaufmann, M.3    Strebhardt, K.4
  • 69
    • 0037046495 scopus 로고    scopus 로고
    • Downregulation of human polo-like kinase activity by antisense oligonucleotides induces growth inhibition in cancer cells
    • 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: 3162-3171.
    • (2002) Oncogene , vol.21 , pp. 3162-3171
    • Spankuch-Schmitt, B.1    Wolf, G.2    Solbach, C.3


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