메뉴 건너뛰기




Volumn 49, Issue 16, 2013, Pages 3547-3558

The HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin modulates radiosensitivity by downregulating serine/threonine kinase 38 via Sp1 inhibition

Author keywords

17 AAG; Radiosensitization; Sp1; STK38

Indexed keywords

HEAT SHOCK PROTEIN 90 INHIBITOR; PROTEIN SERINE THREONINE KINASE; TANESPIMYCIN; TRANSCRIPTION FACTOR SP1;

EID: 84885191034     PISSN: 09598049     EISSN: 18790852     Source Type: Journal    
DOI: 10.1016/j.ejca.2013.06.034     Document Type: Article
Times cited : (23)

References (39)
  • 2
    • 0037862059 scopus 로고    scopus 로고
    • NDR family of AGC kinases - Essential regulators of the cell cycle and morphogenesis
    • R. Tamaskovic, S.J. Bichsel, and B.A. Hemmings NDR family of AGC kinases - essential regulators of the cell cycle and morphogenesis FEBS Lett 546 2003 73 80
    • (2003) FEBS Lett , vol.546 , pp. 73-80
    • Tamaskovic, R.1    Bichsel, S.J.2    Hemmings, B.A.3
  • 4
    • 0032560523 scopus 로고    scopus 로고
    • Fission yeast orb6, a ser/thr protein kinase related to mammalian rho kinase and myotonic dystrophy kinase, is required for maintenance of cell polarity and coordinates cell morphogenesis with the cell cycle
    • F. Verde, D.J. Wiley, and P. Nurse Fission yeast orb6, a ser/thr protein kinase related to mammalian rho kinase and myotonic dystrophy kinase, is required for maintenance of cell polarity and coordinates cell morphogenesis with the cell cycle Proc Natl Acad Sci USA 95 1998 7526 7531
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7526-7531
    • Verde, F.1    Wiley, D.J.2    Nurse, P.3
  • 5
    • 0035102799 scopus 로고    scopus 로고
    • The Cbk1p pathway is important for polarized cell growth and cell separation in Saccharomyces cerevisiae
    • S. Bidlingmaier, E.L. Weiss, C. Seidel, D.G. Drubin, and M. Snyder The Cbk1p pathway is important for polarized cell growth and cell separation in Saccharomyces cerevisiae Mol Cell Biol 21 2001 2449 2462
    • (2001) Mol Cell Biol , vol.21 , pp. 2449-2462
    • Bidlingmaier, S.1    Weiss, E.L.2    Seidel, C.3    Drubin, D.G.4    Snyder, M.5
  • 6
    • 0025210546 scopus 로고
    • The product of the Saccharomyces cerevisiae cell cycle gene DBF2 has homology with protein kinases and is periodically expressed in the cell cycle
    • L.H. Johnston, S.L. Eberly, J.W. Chapman, H. Araki, and A. Sugino The product of the Saccharomyces cerevisiae cell cycle gene DBF2 has homology with protein kinases and is periodically expressed in the cell cycle Mol Cell Biol 10 1990 1358 1366
    • (1990) Mol Cell Biol , vol.10 , pp. 1358-1366
    • Johnston, L.H.1    Eberly, S.L.2    Chapman, J.W.3    Araki, H.4    Sugino, A.5
  • 7
    • 2542482742 scopus 로고    scopus 로고
    • Regulation of NDR2 protein kinase by multi-site phosphorylation and the S100B calcium-binding protein
    • M.R. Stegert, R. Tamaskovic, S.J. Bichsel, A. Hergovich, and B.A. Hemmings Regulation of NDR2 protein kinase by multi-site phosphorylation and the S100B calcium-binding protein J Biol Chem 279 2005 23806 23812
    • (2005) J Biol Chem , vol.279 , pp. 23806-23812
    • Stegert, M.R.1    Tamaskovic, R.2    Bichsel, S.J.3    Hergovich, A.4    Hemmings, B.A.5
  • 8
    • 84863347402 scopus 로고    scopus 로고
    • Chemical genetic identification of NDR1/2 kinase substrates AAK1 and Rabin8 uncovers their roles in dendrite arborization and spine development
    • S.K. Ultanir, N.T. Hertz, and G. Li Chemical genetic identification of NDR1/2 kinase substrates AAK1 and Rabin8 uncovers their roles in dendrite arborization and spine development Neuron 73 2012 1127 1142
    • (2012) Neuron , vol.73 , pp. 1127-1142
    • Ultanir, S.K.1    Hertz, N.T.2    Li, G.3
  • 9
    • 28544435761 scopus 로고    scopus 로고
    • Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3
    • M.R. Stegert, A. Hergovich, R. Tamaskovic, S.J. Bichsel, and B.A. Hemmings Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3 Mol Cell Biol 25 2005 11019 11029
    • (2005) Mol Cell Biol , vol.25 , pp. 11019-11029
    • Stegert, M.R.1    Hergovich, A.2    Tamaskovic, R.3    Bichsel, S.J.4    Hemmings, B.A.5
  • 10
    • 4143117852 scopus 로고    scopus 로고
    • Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein
    • S.J. Bichsel, R. Tamaskovic, M.R. Stegert, and B.A. Hemmings Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein J Biol Chem 279 2004 35228 35235
    • (2004) J Biol Chem , vol.279 , pp. 35228-35235
    • Bichsel, S.J.1    Tamaskovic, R.2    Stegert, M.R.3    Hemmings, B.A.4
  • 11
    • 2642546543 scopus 로고    scopus 로고
    • Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases
    • E. Devroe, H. Erdjument-Bromage, P. Tempst, and P.A. Silver Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases J Biol Chem 279 2004 24444 24451
    • (2004) J Biol Chem , vol.279 , pp. 24444-24451
    • Devroe, E.1    Erdjument-Bromage, H.2    Tempst, P.3    Silver, P.A.4
  • 12
    • 84855469155 scopus 로고    scopus 로고
    • Serine-threonine kinase 38 is regulated by glycogen synthase kinase-3 and modulates oxidative stress-induced cell death
    • A. Enomoto, N. Kido, M. Ito, N. Takamatsu, and K. Miyagawa Serine-threonine kinase 38 is regulated by glycogen synthase kinase-3 and modulates oxidative stress-induced cell death Free Radic Biol Med 52 2012 507 515
    • (2012) Free Radic Biol Med , vol.52 , pp. 507-515
    • Enomoto, A.1    Kido, N.2    Ito, M.3    Takamatsu, N.4    Miyagawa, K.5
  • 13
    • 41149105368 scopus 로고    scopus 로고
    • Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 (STK38)
    • A. Enomoto, N. Kido, and M. Ito Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 (STK38) Oncogene 27 2008 1930 1938
    • (2008) Oncogene , vol.27 , pp. 1930-1938
    • Enomoto, A.1    Kido, N.2    Ito, M.3
  • 15
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • L.H. Pearl, C. Prodromou, and P. Workman The Hsp90 molecular chaperone: an open and shut case for treatment Biochem J 410 2008 439 453
    • (2008) Biochem J , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 17
    • 74249085361 scopus 로고    scopus 로고
    • Update on Hsp90 inhibitors in clinical trial
    • Y.S. Kim, S.V. Alarcon, and S. Lee Update on Hsp90 inhibitors in clinical trial Curr Top Med Chem 9 2009 1479 1492
    • (2009) Curr Top Med Chem , vol.9 , pp. 1479-1492
    • Kim, Y.S.1    Alarcon, S.V.2    Lee, S.3
  • 18
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • L. Whitesell, and S.L. Lindquist HSP90 and the chaperoning of cancer Nat Rev Cancer 5 2005 761 772
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 19
    • 33746191768 scopus 로고    scopus 로고
    • Inhibitors of the HSP90 molecular chaperone: Current status
    • S. Sharp, and P. Workman Inhibitors of the HSP90 molecular chaperone: current status Adv Cancer Res 95 2006 323 348
    • (2006) Adv Cancer Res , vol.95 , pp. 323-348
    • Sharp, S.1    Workman, P.2
  • 20
    • 0036219609 scopus 로고    scopus 로고
    • Hsp90 inhibitors as novel cancer chemotherapeutic agents
    • L. Neckers Hsp90 inhibitors as novel cancer chemotherapeutic agents Trends Mol Med 8 2002 S55 S61
    • (2002) Trends Mol Med , vol.8
    • Neckers, L.1
  • 21
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of Hsp90 confers tumor selectivity on Hsp90 inhibitors
    • A. Kamal, L. Thao, and J. Sensintaffar A high-affinity conformation of Hsp90 confers tumor selectivity on Hsp90 inhibitors Nature 425 2003 407 410
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3
  • 22
    • 44449168998 scopus 로고    scopus 로고
    • Radiosensitization of human vascular endothelial cells through Hsp90 inhibition with 17-N-allilamino-17-demethoxygeldanamycin
    • A.E. Kabakov, Y.M. Makarova, and Y.V. Malyutina Radiosensitization of human vascular endothelial cells through Hsp90 inhibition with 17-N-allilamino-17-demethoxygeldanamycin Int J Radiat Oncol Biol Phys 71 2008 858 865
    • (2008) Int J Radiat Oncol Biol Phys , vol.71 , pp. 858-865
    • Kabakov, A.E.1    Makarova, Y.M.2    Malyutina, Y.V.3
  • 23
    • 33750696349 scopus 로고    scopus 로고
    • Inhibition of homologous recombination repair in irradiated tumor cells pretreated with Hsp90 inhibitor 17-allylamino-17demethoxygeldanamycin
    • M. Noguchi, D. Yu, and R. Hirayama Inhibition of homologous recombination repair in irradiated tumor cells pretreated with Hsp90 inhibitor 17-allylamino-17demethoxygeldanamycin Biochem Biophys Res Commun 351 2006 658 663
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 658-663
    • Noguchi, M.1    Yu, D.2    Hirayama, R.3
  • 24
    • 84865306252 scopus 로고    scopus 로고
    • Brca1 and Hsp90 cooperate in homologous and non-homologous DNA double-strand-break repair and G2/M checkpoint activation
    • S.R. Stecklein, E. Kumaraswamy, and F. Behbod Brca1 and Hsp90 cooperate in homologous and non-homologous DNA double-strand-break repair and G2/M checkpoint activation Proc Natl Acad Sci USA 109 2012 13650 13655
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 13650-13655
    • Stecklein, S.R.1    Kumaraswamy, E.2    Behbod, F.3
  • 25
    • 52149120751 scopus 로고    scopus 로고
    • Geldanamycin promotes premature mitotic entry and micronucleation in irradiated p53/p21 deficient colon carcinoma cells
    • D.M. Moran, G. Gawlak, M.S. Jayaprakash, S. Mayar, and C.G. Maki Geldanamycin promotes premature mitotic entry and micronucleation in irradiated p53/p21 deficient colon carcinoma cells Oncogene 27 2008 5567 5577
    • (2008) Oncogene , vol.27 , pp. 5567-5577
    • Moran, D.M.1    Gawlak, G.2    Jayaprakash, M.S.3    Mayar, S.4    Maki, C.G.5
  • 26
    • 78449273417 scopus 로고    scopus 로고
    • Heat shock protein 90 inhibition depletes LATS1 and LATS2, two regulators of the mammalian hippo tumor suppressor pathway
    • C.J. Huntoon, M.D. Nye, and L. Geng Heat shock protein 90 inhibition depletes LATS1 and LATS2, two regulators of the mammalian hippo tumor suppressor pathway Cancer Res 70 2010 8642 8650
    • (2010) Cancer Res , vol.70 , pp. 8642-8650
    • Huntoon, C.J.1    Nye, M.D.2    Geng, L.3
  • 27
    • 0032866999 scopus 로고    scopus 로고
    • The Sp-family of transcription factors
    • G. Suske The Sp-family of transcription factors Gene 238 1999 291 300
    • (1999) Gene , vol.238 , pp. 291-300
    • Suske, G.1
  • 28
    • 0037150687 scopus 로고    scopus 로고
    • Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease
    • A.W. Dunah, H. Jeong, and A. Griffin Sp1 and TAFII130 transcriptional activity disrupted in early Huntington's disease Science 296 2002 2238 2243
    • (2002) Science , vol.296 , pp. 2238-2243
    • Dunah, A.W.1    Jeong, H.2    Griffin, A.3
  • 29
    • 63449115498 scopus 로고    scopus 로고
    • Heat shock protein 90 is important for Sp1 stability during mitosis
    • S.A. Wang, J.Y. Chuang, and S.H. Yeh Heat shock protein 90 is important for Sp1 stability during mitosis J Mol Biol 387 2009 1106 1119
    • (2009) J Mol Biol , vol.387 , pp. 1106-1119
    • Wang, S.A.1    Chuang, J.Y.2    Yeh, S.H.3
  • 30
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAPK kinases
    • R.J. Davis Signal transduction by the JNK group of MAPK kinases Cell 103 2000 239 252
    • (2000) Cell , vol.103 , pp. 239-252
    • Davis, R.J.1
  • 32
    • 33847737716 scopus 로고    scopus 로고
    • DNA damage checkpoints: From initiation to recovery or adaptation
    • J. Bartek, and J. Lukas DNA damage checkpoints: from initiation to recovery or adaptation Curr Opin Cell Biol 19 2007 238 245
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 238-245
    • Bartek, J.1    Lukas, J.2
  • 33
    • 0141568014 scopus 로고    scopus 로고
    • Enhanced cell killing induced by the combination of radiation and the heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin: A multitarget approach to radiosensitization
    • J.S. Russel, W. Burgan, K.A. Oswald, K. Camphausen, and P.J. Tofilon Enhanced cell killing induced by the combination of radiation and the heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin: a multitarget approach to radiosensitization Clin Cancer Res 9 2003 3794 3800
    • (2003) Clin Cancer Res , vol.9 , pp. 3794-3800
    • Russel, J.S.1    Burgan, W.2    Oswald, K.A.3    Camphausen, K.4    Tofilon, P.J.5
  • 34
    • 60549083336 scopus 로고    scopus 로고
    • Targeting heat shock protein 90 overrides the resistance of lung cancer cells by blocking radiation-induced stabilization of hypoxia-inducible factor-1α
    • W.Y. Kim, S.H. Oh, J.K. Woo, W.K. Hong, and H.Y. Lee Targeting heat shock protein 90 overrides the resistance of lung cancer cells by blocking radiation-induced stabilization of hypoxia-inducible factor-1α Cancer Res 69 2009 1624 1632
    • (2009) Cancer Res , vol.69 , pp. 1624-1632
    • Kim, W.Y.1    Oh, S.H.2    Woo, J.K.3    Hong, W.K.4    Lee, H.Y.5
  • 35
    • 0034607702 scopus 로고    scopus 로고
    • Requirement of JNK for stress-induced activation of the cytochrome c-mediated death pathway
    • C. Tournier, P. Hess, and D.D. Yang Requirement of JNK for stress-induced activation of the cytochrome c-mediated death pathway Science 288 2000 870 874
    • (2000) Science , vol.288 , pp. 870-874
    • Tournier, C.1    Hess, P.2    Yang, D.D.3
  • 36
    • 84887498337 scopus 로고    scopus 로고
    • STK38 is a critical upstream regulator of Myc's oncogenic activity in human B-cell lymphoma
    • advance online publication, 26 November, 2012
    • B.C. Bisikirska, S.J. Adam, and M.J. Alvarez STK38 is a critical upstream regulator of Myc's oncogenic activity in human B-cell lymphoma Oncogene 2012 advance online publication, 26 November, 2012
    • (2012) Oncogene
    • Bisikirska, B.C.1    Adam, S.J.2    Alvarez, M.J.3
  • 37
    • 33847080309 scopus 로고    scopus 로고
    • Centrosome-associated NDR kinase regulates centrosome duplication
    • A. Hergovich, S. Lamla, E.A. Nigg, and B.A. Hemmings Centrosome- associated NDR kinase regulates centrosome duplication Mol Cell 25 2007 625 634
    • (2007) Mol Cell , vol.25 , pp. 625-634
    • Hergovich, A.1    Lamla, S.2    Nigg, E.A.3    Hemmings, B.A.4
  • 38
    • 0032531742 scopus 로고    scopus 로고
    • Calcium regulation of Ndr protein kinase mediated by S100 calcium-binding proteins
    • T.A. Millward, C.W. Heizmann, B.W. Schafer, and B.A. Hemmings Calcium regulation of Ndr protein kinase mediated by S100 calcium-binding proteins EMBO J 17 1998 5913 5922
    • (1998) EMBO J , vol.17 , pp. 5913-5922
    • Millward, T.A.1    Heizmann, C.W.2    Schafer, B.W.3    Hemmings, B.A.4
  • 39
    • 0036898616 scopus 로고    scopus 로고
    • Analysis of gene expression in ductal carcinoma in situ of the breast
    • A. Adeyinka, E. Emberley, and Y. Niu Analysis of gene expression in ductal carcinoma in situ of the breast Clin Cancer Res 8 2002 3788 3795 Technology
    • (2002) Clin Cancer Res , vol.8 , pp. 3788-3795
    • Adeyinka, A.1    Emberley, E.2    Niu, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.