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Volumn 7, Issue , 2016, Pages e2039-

Deubiquitylating enzyme USP9x regulates radiosensitivity in glioblastoma cells by Mcl-1-dependent and -independent mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

BETA ACTIN; BIM PROTEIN; DEUBIQUITINASE; POLYUBIQUITIN; PROTEIN BAD; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN MCL 1; PROTEIN NOXA; PUMA PROTEIN; SMALL INTERFERING RNA; UBIQUITIN SPECIFIC PROTEASE 9X; UNCLASSIFIED DRUG; UBIQUITIN THIOLESTERASE; USP9X PROTEIN, HUMAN;

EID: 84955117020     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2015.405     Document Type: Article
Times cited : (34)

References (44)
  • 1
    • 0034708169 scopus 로고    scopus 로고
    • Differential role of caspase-8 and BID activation during radiation- and CD95-induced apoptosis
    • Belka C, Rudner J, Wesselborg S, Stepczynska A, Marini P, Lepple-Wienhues A et al. Differential role of caspase-8 and BID activation during radiation- and CD95-induced apoptosis. Oncogene 2000; 19: 1181-1190.
    • (2000) Oncogene , vol.19 , pp. 1181-1190
    • Belka, C.1    Rudner, J.2    Wesselborg, S.3    Stepczynska, A.4    Marini, P.5    Lepple-Wienhues, A.6
  • 2
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle RJ, Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 2008; 9: 47-59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 3
    • 33847328289 scopus 로고    scopus 로고
    • The Bcl-2 apoptotic switch in cancer development and therapy
    • Adams JM, Cory S. The Bcl-2 apoptotic switch in cancer development and therapy. Oncogene 2007; 26: 1324-1337.
    • (2007) Oncogene , vol.26 , pp. 1324-1337
    • Adams, J.M.1    Cory, S.2
  • 4
    • 80051761743 scopus 로고    scopus 로고
    • The role of Bcl-2 and its pro-survival relatives in tumourigenesis and cancer therapy
    • Kelly PN, Strasser A. The role of Bcl-2 and its pro-survival relatives in tumourigenesis and cancer therapy. Cell Death Differ 2011; 18: 1414-1424.
    • (2011) Cell Death Differ , vol.18 , pp. 1414-1424
    • Kelly, P.N.1    Strasser, A.2
  • 5
    • 56149097601 scopus 로고    scopus 로고
    • Apoptosis-based treatment of glioblastomas with ABT-737, a novel small molecule inhibitor of Bcl-2 family proteins
    • Tagscherer KE, Fassl A, Campos B, Farhadi M, Kraemer A, Bock BC et al. Apoptosis-based treatment of glioblastomas with ABT-737, a novel small molecule inhibitor of Bcl-2 family proteins. Oncogene 2008; 27: 6646-6656.
    • (2008) Oncogene , vol.27 , pp. 6646-6656
    • Tagscherer, K.E.1    Fassl, A.2    Campos, B.3    Farhadi, M.4    Kraemer, A.5    Bock, B.C.6
  • 6
    • 33750834023 scopus 로고    scopus 로고
    • The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized
    • van Delft MF, Wei AH, Mason KD, Vandenberg CJ, Chen L, Czabotar PE et al. The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized. Cancer Cell 2006; 10: 389-399.
    • (2006) Cancer Cell , vol.10 , pp. 389-399
    • Van Delft, M.F.1    Wei, A.H.2    Mason, K.D.3    Vandenberg, C.J.4    Chen, L.5    Czabotar, P.E.6
  • 8
    • 79955809893 scopus 로고    scopus 로고
    • Sorafenib induces cell death in chronic lymphocytic leukemia by translational downregulation of Mcl-1
    • Huber S, Oelsner M, Decker T, zum Buschenfelde CM, Wagner M, Lutzny G et al. Sorafenib induces cell death in chronic lymphocytic leukemia by translational downregulation of Mcl-1. Leukemia 2011; 25: 838-847.
    • (2011) Leukemia , vol.25 , pp. 838-847
    • Huber, S.1    Oelsner, M.2    Decker, T.3    Zum Buschenfelde, C.M.4    Wagner, M.5    Lutzny, G.6
  • 9
    • 84867806661 scopus 로고    scopus 로고
    • Deubiquitinase USP9x confers radioresistance through stabilization of Mcl-1
    • Trivigno D, Essmann F, Huber SM, Rudner J. Deubiquitinase USP9x confers radioresistance through stabilization of Mcl-1. Neoplasia 2012; 14: 893-904.
    • (2012) Neoplasia , vol.14 , pp. 893-904
    • Trivigno, D.1    Essmann, F.2    Huber, S.M.3    Rudner, J.4
  • 10
    • 33644855216 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1
    • Maurer U, Charvet C, Wagman AS, Dejardin E, Green DR. Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1. Mol Cell 2006; 21: 749-760.
    • (2006) Mol Cell , vol.21 , pp. 749-760
    • Maurer, U.1    Charvet, C.2    Wagman, A.S.3    Dejardin, E.4    Green, D.R.5
  • 11
    • 79952261405 scopus 로고    scopus 로고
    • SCF(FBW7) regulates cellular apoptosis by targeting MCL1 for ubiquitylation and destruction
    • Inuzuka H, Shaik S, Onoyama I, Gao D, Tseng A, Maser RS et al. SCF(FBW7) regulates cellular apoptosis by targeting MCL1 for ubiquitylation and destruction. Nature 2011; 471: 104-109.
    • (2011) Nature , vol.471 , pp. 104-109
    • Inuzuka, H.1    Shaik, S.2    Onoyama, I.3    Gao, D.4    Tseng, A.5    Maser, R.S.6
  • 12
    • 73849083434 scopus 로고    scopus 로고
    • Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
    • Schwickart M, Huang X, Lill JR, Liu J, Ferrando R, French DM et al. Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 2010; 463: 103-107.
    • (2010) Nature , vol.463 , pp. 103-107
    • Schwickart, M.1    Huang, X.2    Lill, J.R.3    Liu, J.4    Ferrando, R.5    French, D.M.6
  • 13
    • 73349134695 scopus 로고    scopus 로고
    • NOA-04 randomized phase III trial of sequential radiochemotherapy of anaplastic glioma with procarbazine, lomustine, and vincristine or temozolomide
    • Wick W, Hartmann C, Engel C, Stoffels M, Felsberg J, Stockhammer F et al. NOA-04 randomized phase III trial of sequential radiochemotherapy of anaplastic glioma with procarbazine, lomustine, and vincristine or temozolomide. J Clin Oncol 2009; 27: 5874-5880.
    • (2009) J Clin Oncol , vol.27 , pp. 5874-5880
    • Wick, W.1    Hartmann, C.2    Engel, C.3    Stoffels, M.4    Felsberg, J.5    Stockhammer, F.6
  • 14
    • 84862500662 scopus 로고    scopus 로고
    • p53-dependent regulation of Mcl-1 contributes to synergistic cell death by ionizing radiation and the Bcl-2/Bcl-XL inhibitor ABT-737
    • Tagscherer KE, Fassl A, Sinkovic T, Combs SE, Roth W. p53-dependent regulation of Mcl-1 contributes to synergistic cell death by ionizing radiation and the Bcl-2/Bcl-XL inhibitor ABT-737. Apoptosis 2012; 17: 187-199.
    • (2012) Apoptosis , vol.17 , pp. 187-199
    • Tagscherer, K.E.1    Fassl, A.2    Sinkovic, T.3    Combs, S.E.4    Roth, W.5
  • 15
    • 79960146856 scopus 로고    scopus 로고
    • Synergistic antitumor activity of gemcitabine and ABT-737 in vitro and in vivo through disrupting the interaction of USP9X and Mcl-1
    • Zhang C, Cai TY, Zhu H, Yang LQ, Jiang H, Dong XW et al. Synergistic antitumor activity of gemcitabine and ABT-737 in vitro and in vivo through disrupting the interaction of USP9X and Mcl-1. Mol Cancer Ther 2011; 10: 1264-1275.
    • (2011) Mol Cancer Ther , vol.10 , pp. 1264-1275
    • Zhang, C.1    Cai, T.Y.2    Zhu, H.3    Yang, L.Q.4    Jiang, H.5    Dong, X.W.6
  • 16
    • 84869217978 scopus 로고    scopus 로고
    • The downregulation of Mcl-1 via USP9X inhibition sensitizes solid tumors to Bcl-xl inhibition
    • Peddaboina C, Jupiter D, Fletcher S, Yap JL, Rai A, Tobin RP et al. The downregulation of Mcl-1 via USP9X inhibition sensitizes solid tumors to Bcl-xl inhibition. BMC Cancer 2012; 12: 541.
    • (2012) BMC Cancer , vol.12 , pp. 541
    • Peddaboina, C.1    Jupiter, D.2    Fletcher, S.3    Yap, J.L.4    Rai, A.5    Tobin, R.P.6
  • 17
    • 84901197944 scopus 로고    scopus 로고
    • Bak and Mcl-1 are essential for temozolomide induced cell death in human glioma
    • Gratas C, Sery Q, Rabe M, Oliver L, Vallette FM. Bak and Mcl-1 are essential for temozolomide induced cell death in human glioma. Oncotarget 2014; 5: 2428-2435.
    • (2014) Oncotarget , vol.5 , pp. 2428-2435
    • Gratas, C.1    Sery, Q.2    Rabe, M.3    Oliver, L.4    Vallette, F.M.5
  • 19
    • 79952160999 scopus 로고    scopus 로고
    • c-Abl regulates Mcl-1 gene expression in chronic lymphocytic leukemia cells
    • Allen JC, Talab F, Zuzel M, Lin K, Slupsky JR. c-Abl regulates Mcl-1 gene expression in chronic lymphocytic leukemia cells. Blood 2011; 117: 2414-2422.
    • (2011) Blood , vol.117 , pp. 2414-2422
    • Allen, J.C.1    Talab, F.2    Zuzel, M.3    Lin, K.4    Slupsky, J.R.5
  • 20
    • 34347350211 scopus 로고    scopus 로고
    • Degradation of Mcl-1 by beta-TrCP mediates glycogen synthase kinase 3-induced tumor suppression and chemosensitization
    • Ding Q, He X, Hsu JM, Xia W, Chen CT, Li LY et al. Degradation of Mcl-1 by beta-TrCP mediates glycogen synthase kinase 3-induced tumor suppression and chemosensitization. Mol Cell Biol 2007; 27: 4006-4017.
    • (2007) Mol Cell Biol , vol.27 , pp. 4006-4017
    • Ding, Q.1    He, X.2    Hsu, J.M.3    Xia, W.4    Chen, C.T.5    Li, L.Y.6
  • 21
    • 79952271269 scopus 로고    scopus 로고
    • Sensitivity to antitubulin chemotherapeutics is regulated by MCL1 and FBW7
    • Wertz IE, Kusam S, Lam C, Okamoto T, Sandoval W, Anderson DJ et al. Sensitivity to antitubulin chemotherapeutics is regulated by MCL1 and FBW7. Nature 2011; 471: 110-114.
    • (2011) Nature , vol.471 , pp. 110-114
    • Wertz, I.E.1    Kusam, S.2    Lam, C.3    Okamoto, T.4    Sandoval, W.5    Anderson, D.J.6
  • 22
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • Zhong Q, Gao W, Du F, Wang X. Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 2005; 121: 1085-1095.
    • (2005) Cell , vol.121 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4
  • 24
    • 84877113183 scopus 로고    scopus 로고
    • The SOX2-interactome in brain cancer cells identifies the requirement of MSI2 and USP9X for the growth of brain tumor cells
    • Cox JL, Wilder PJ, Gilmore JM, Wuebben EL, Washburn MP, Rizzino A. The SOX2-interactome in brain cancer cells identifies the requirement of MSI2 and USP9X for the growth of brain tumor cells. PloS One 2013; 8: e62857.
    • (2013) PloS One , vol.8
    • Cox, J.L.1    Wilder, P.J.2    Gilmore, J.M.3    Wuebben, E.L.4    Washburn, M.P.5    Rizzino, A.6
  • 25
    • 84879824271 scopus 로고    scopus 로고
    • Loss of Usp9x disrupts cortical architecture, hippocampal development and TGFbeta-mediated axonogenesis
    • Stegeman S, Jolly LA, Premarathne S, Gecz J, Richards LJ, Mackay-Sim A et al. Loss of Usp9x disrupts cortical architecture, hippocampal development and TGFbeta-mediated axonogenesis. PloS One 2013; 8: e68287.
    • (2013) PloS One , vol.8
    • Stegeman, S.1    Jolly, L.A.2    Premarathne, S.3    Gecz, J.4    Richards, L.J.5    Mackay-Sim, A.6
  • 26
    • 84896768982 scopus 로고    scopus 로고
    • Mutations in USP9X are associated with X-linked intellectual disability and disrupt neuronal cell migration and growth
    • Homan CC, Kumar R, Nguyen LS, Haan E, Raymond FL, Abidi F et al. Mutations in USP9X are associated with X-linked intellectual disability and disrupt neuronal cell migration and growth. Am J Hum Genet 2014; 94: 470-478.
    • (2014) Am J Hum Genet , vol.94 , pp. 470-478
    • Homan, C.C.1    Kumar, R.2    Nguyen, L.S.3    Haan, E.4    Raymond, F.L.5    Abidi, F.6
  • 27
    • 33846019272 scopus 로고    scopus 로고
    • The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X
    • Mouchantaf R, Azakir BA, McPherson PS, Millard SM, Wood SA, Angers A. The ubiquitin ligase itch is auto-ubiquitylated in vivo and in vitro but is protected from degradation by interacting with the deubiquitylating enzyme FAM/USP9X. J Biol Chem 2006; 281: 38738-38747.
    • (2006) J Biol Chem , vol.281 , pp. 38738-38747
    • Mouchantaf, R.1    Azakir, B.A.2    McPherson, P.S.3    Millard, S.M.4    Wood, S.A.5    Angers, A.6
  • 28
    • 0033392501 scopus 로고    scopus 로고
    • The deubiquitinating enzyme Fam interacts with and stabilizes beta-catenin
    • Taya S, Yamamoto T, Kanai-Azuma M, Wood SA, Kaibuchi K. The deubiquitinating enzyme Fam interacts with and stabilizes beta-catenin. Genes Cells 1999; 4: 757-767.
    • (1999) Genes Cells , vol.4 , pp. 757-767
    • Taya, S.1    Yamamoto, T.2    Kanai-Azuma, M.3    Wood, S.A.4    Kaibuchi, K.5
  • 30
    • 67349180984 scopus 로고    scopus 로고
    • Reciprocal regulation of the ubiquitin ligase Itch and the epidermal growth factor receptor signaling
    • Azakir BA, Angers A. Reciprocal regulation of the ubiquitin ligase Itch and the epidermal growth factor receptor signaling. Cell Signal 2009; 21: 1326-1336.
    • (2009) Cell Signal , vol.21 , pp. 1326-1336
    • Azakir, B.A.1    Angers, A.2
  • 32
    • 84903769379 scopus 로고    scopus 로고
    • Prolyl hydroxylation by EglN2 destabilizes FOXO3a by blocking its interaction with the USP9x deubiquitinase
    • Zheng X, Zhai B, Koivunen P, Shin SJ, Lu G, Liu J et al. Prolyl hydroxylation by EglN2 destabilizes FOXO3a by blocking its interaction with the USP9x deubiquitinase. Genes Dev 2014; 28: 1429-1444.
    • (2014) Genes Dev , vol.28 , pp. 1429-1444
    • Zheng, X.1    Zhai, B.2    Koivunen, P.3    Shin, S.J.4    Lu, G.5    Liu, J.6
  • 33
    • 0031059570 scopus 로고    scopus 로고
    • Immunohistochemical analysis of Bcl-2, Bcl-X, Mcl-1, and Bax in tumors of central and peripheral nervous system origin
    • Krajewski S, Krajewska M, Ehrmann J, Sikorska M, Lach B, Chatten J et al. Immunohistochemical analysis of Bcl-2, Bcl-X, Mcl-1, and Bax in tumors of central and peripheral nervous system origin. Am J Pathol 1997; 150: 805-814.
    • (1997) Am J Pathol , vol.150 , pp. 805-814
    • Krajewski, S.1    Krajewska, M.2    Ehrmann, J.3    Sikorska, M.4    Lach, B.5    Chatten, J.6
  • 34
    • 84924697369 scopus 로고    scopus 로고
    • Potent and selective small-molecule MCL-1 inhibitors demonstrate on-target cancer cell killing activity as single agents and in combination with ABT-263 (navitoclax)
    • Leverson JD, Zhang H, Chen J, Tahir SK, Phillips DC, Xue J et al. Potent and selective small-molecule MCL-1 inhibitors demonstrate on-target cancer cell killing activity as single agents and in combination with ABT-263 (navitoclax). Cell Death Dis 2015; 6: e1590.
    • (2015) Cell Death Dis , vol.6
    • Leverson, J.D.1    Zhang, H.2    Chen, J.3    Tahir, S.K.4    Phillips, D.C.5    Xue, J.6
  • 35
    • 84904267338 scopus 로고    scopus 로고
    • PI3K and Bcl-2 inhibition primes glioblastoma cells to apoptosis through downregulation of Mcl-1 and Phospho-BAD
    • Pareja F, Macleod D, Shu C, Crary JF, Canoll PD, Ross AH et al. PI3K and Bcl-2 inhibition primes glioblastoma cells to apoptosis through downregulation of Mcl-1 and Phospho-BAD. Mol Cancer Res 2014; 12: 987-1001.
    • (2014) Mol Cancer Res , vol.12 , pp. 987-1001
    • Pareja, F.1    Macleod, D.2    Shu, C.3    Crary, J.F.4    Canoll, P.D.5    Ross, A.H.6
  • 36
    • 84877850185 scopus 로고    scopus 로고
    • ABT-263 enhances sensitivity to metformin and 2-deoxyglucose in pediatric glioma by promoting apoptotic cell death
    • Levesley J, Steele L, Taylor C, Sinha P, Lawler SE. ABT-263 enhances sensitivity to metformin and 2-deoxyglucose in pediatric glioma by promoting apoptotic cell death. PloS One 2013; 8: e64051.
    • (2013) PloS One , vol.8
    • Levesley, J.1    Steele, L.2    Taylor, C.3    Sinha, P.4    Lawler, S.E.5
  • 38
    • 33646354381 scopus 로고    scopus 로고
    • Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members
    • Certo M, Del Gaizo Moore V, Nishino M, Wei G, Korsmeyer S, Armstrong SA et al. Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members. Cancer Cell 2006; 9: 351-365.
    • (2006) Cancer Cell , vol.9 , pp. 351-365
    • Certo, M.1    Del Gaizo Moore, V.2    Nishino, M.3    Wei, G.4    Korsmeyer, S.5    Armstrong, S.A.6
  • 39
    • 84942991698 scopus 로고    scopus 로고
    • An interconnected hierarchical model of cell death regulation by the BCL-2 family
    • Chen HC, Kanai M, Inoue-Yamauchi A, Tu HC, Huang Y, Ren D et al. An interconnected hierarchical model of cell death regulation by the BCL-2 family. Nat Cell Biol 2015; 17: 1270-1281.
    • (2015) Nat Cell Biol , vol.17 , pp. 1270-1281
    • Chen, H.C.1    Kanai, M.2    Inoue-Yamauchi, A.3    Tu, H.C.4    Huang, Y.5    Ren, D.6
  • 40
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita T, Reed JC. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell 1995; 80: 293-299.
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 41
    • 0034640281 scopus 로고    scopus 로고
    • Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis
    • Oda E, Ohki R, Murasawa H, Nemoto J, Shibue T, Yamashita T et al. Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis. Science 2000; 288: 1053-1058.
    • (2000) Science , vol.288 , pp. 1053-1058
    • Oda, E.1    Ohki, R.2    Murasawa, H.3    Nemoto, J.4    Shibue, T.5    Yamashita, T.6
  • 42
    • 0027319521 scopus 로고
    • p53 is required for radiationinduced apoptosis in mouse thymocytes
    • Lowe SW, Schmitt EM, Smith SW, Osborne BA, Jacks T. p53 is required for radiationinduced apoptosis in mouse thymocytes. Nature 1993; 362: 847-849.
    • (1993) Nature , vol.362 , pp. 847-849
    • Lowe, S.W.1    Schmitt, E.M.2    Smith, S.W.3    Osborne, B.A.4    Jacks, T.5
  • 43
    • 84881475565 scopus 로고    scopus 로고
    • Current understanding of the role and targeting of tumor suppressor p53 in glioblastoma multiforme
    • England B, Huang T, Karsy M. Current understanding of the role and targeting of tumor suppressor p53 in glioblastoma multiforme. Tumour Biol 2013; 34: 2063-2074.
    • (2013) Tumour Biol , vol.34 , pp. 2063-2074
    • England, B.1    Huang, T.2    Karsy, M.3
  • 44
    • 84904703922 scopus 로고    scopus 로고
    • Dihydroartemisinin is a hypoxiaactive anti-cancer drug in colorectal carcinoma cells
    • Ontikatze T, Rudner J, Handrick R, Belka C, Jendrossek V. Dihydroartemisinin is a hypoxiaactive anti-cancer drug in colorectal carcinoma cells. Front Oncol 2014; 4: 116.
    • (2014) Front Oncol , vol.4 , pp. 116
    • Ontikatze, T.1    Rudner, J.2    Handrick, R.3    Belka, C.4    Jendrossek, V.5


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