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Volumn 77, Issue 2, 2017, Pages 343-354

Correction: Molecular chaperone Hsp90 is necessary to prevent cellular senescence VI lysosomal degradation of p14ARF (Cancer Research (2017) 77 (343–354) DOI: 10.1158/0008-5472.CAN-16-0613);Molecular chaperone HSP90 is necessary to prevent cellular senescence via lysosomal degradation of p14ARF

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CYCLIN DEPENDENT KINASE INHIBITOR 2A; GELDANAMYCIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; LYSOSOME ENZYME; STUB1 PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE;

EID: 85018654211     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-18-3311     Document Type: Erratum
Times cited : (23)

References (50)
  • 3
    • 0033591014 scopus 로고    scopus 로고
    • Annual report to the nation on the status of cancer, 1973-1996, with a special section on lung cancer and tobacco smoking
    • Wingo PA, Ries LA, Giovino GA, Miller DS, Rosenberg HM, Shopland DR, et al. Annual report to the nation on the status of cancer, 1973-1996, with a special section on lung cancer and tobacco smoking. J Natl Cancer Inst 1999;91:675-90.
    • (1999) J Natl Cancer Inst , vol.91 , pp. 675-690
    • Wingo, P.A.1    Ries, L.A.2    Giovino, G.A.3    Miller, D.S.4    Rosenberg, H.M.5    Shopland, D.R.6
  • 4
    • 0025768416 scopus 로고
    • Neuroendocrine tumors of the lung with proposed criteria for large-cell neuroendocrine carcinoma. An ultrastructural, immunohistochemical, and flow cytometric study of 35 cases
    • Travis WD, Linnoila RI, Tsokos MG, Hitchcock CL, Cutler GBJr, Nieman L, et al. Neuroendocrine tumors of the lung with proposed criteria for large-cell neuroendocrine carcinoma. An ultrastructural, immunohistochemical, and flow cytometric study of 35 cases. Am J Surg Pathol 1991;15:529-53.
    • (1991) Am J Surg Pathol , vol.15 , pp. 529-553
    • Travis, W.D.1    Linnoila, R.I.2    Tsokos, M.G.3    Hitchcock, C.L.4    Cutler, G.B.5    Nieman, L.6
  • 5
    • 33947502512 scopus 로고    scopus 로고
    • Lung cancer in never smokers: A review
    • Subramanian J, Govindan R. Lung cancer in never smokers: a review. J Clin Oncol 2007;25:561-70.
    • (2007) J Clin Oncol , vol.25 , pp. 561-570
    • Subramanian, J.1    Govindan, R.2
  • 8
    • 79951862254 scopus 로고    scopus 로고
    • The evolving role of histology in the management of advanced non-small-cell lung cancer
    • Langer CJ, Besse B, Gualberto A, Brambilla E, Soria JC. The evolving role of histology in the management of advanced non-small-cell lung cancer. J Clin Oncol 2010;28:5311-20.
    • (2010) J Clin Oncol , vol.28 , pp. 5311-5320
    • Langer, C.J.1    Besse, B.2    Gualberto, A.3    Brambilla, E.4    Soria, J.C.5
  • 9
    • 84877679409 scopus 로고    scopus 로고
    • Targeted inhibition of the molecular chaperone Hsp90 overcomes ALK inhibitor resistance in non-small cell lung cancer
    • Sang J, Acquaviva J, Friedland JC, Smith DL, Sequeira M, Zhang C, et al. Targeted inhibition of the molecular chaperone Hsp90 overcomes ALK inhibitor resistance in non-small cell lung cancer. Cancer Discov 2013;3:430-43.
    • (2013) Cancer Discov , vol.3 , pp. 430-443
    • Sang, J.1    Acquaviva, J.2    Friedland, J.C.3    Smith, D.L.4    Sequeira, M.5    Zhang, C.6
  • 10
    • 77950092933 scopus 로고    scopus 로고
    • Transcription-independent ARF regulation in oncogenic stress-mediated p53 responses
    • Chen D, Shan J, Zhu WG, Qin J, Gu W. Transcription-independent ARF regulation in oncogenic stress-mediated p53 responses. Nature 2010;464:624-7.
    • (2010) Nature , vol.464 , pp. 624-627
    • Chen, D.1    Shan, J.2    Zhu, W.G.3    Qin, J.4    Gu, W.5
  • 11
    • 84869016069 scopus 로고    scopus 로고
    • Acceleration of gastric tumorigenesis through MKRN1-mediated posttranslational regulation of p14ARF
    • Ko A, Shin JY, Seo J, Lee KD, Lee EW, Lee MS, et al. Acceleration of gastric tumorigenesis through MKRN1-mediated posttranslational regulation of p14ARF. J Natl Cancer Inst 2012;104:1660-72.
    • (2012) J Natl Cancer Inst , vol.104 , pp. 1660-1672
    • Ko, A.1    Shin, J.Y.2    Seo, J.3    Lee, K.D.4    Lee, E.W.5    Lee, M.S.6
  • 12
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: Emerging mechanistic insights
    • Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol 2010;11:515-28.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 13
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL. HSP90 and the chaperoning of cancer. Nat Rev Cancer 2005;5:761-72.
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 14
    • 2642521990 scopus 로고    scopus 로고
    • Therapeutic and diagnostic implications of Hsp90 activation
    • Kamal A, Boehm MF, Burrows FJ. Therapeutic and diagnostic implications of Hsp90 activation. Trends Mol Med 2004;10:283-90.
    • (2004) Trends Mol Med , vol.10 , pp. 283-290
    • Kamal, A.1    Boehm, M.F.2    Burrows, F.J.3
  • 15
    • 58149271606 scopus 로고    scopus 로고
    • Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms
    • Johnson JL, Brown C. Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms. Cell Stress Chaperones 2009;14:83-94.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 83-94
    • Johnson, J.L.1    Brown, C.2
  • 16
    • 0037075232 scopus 로고    scopus 로고
    • Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2
    • Basso AD, Solit DB, Munster PN, Rosen N. Ansamycin antibiotics inhibit Akt activation and cyclin D expression in breast cancer cells that overexpress HER2. Oncogene 2002;21:1159-66.
    • (2002) Oncogene , vol.21 , pp. 1159-1166
    • Basso, A.D.1    Solit, D.B.2    Munster, P.N.3    Rosen, N.4
  • 17
    • 0035793546 scopus 로고    scopus 로고
    • Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90
    • Xu W, Mimnaugh E, Rosser MF, Nicchitta C, Marcu M, Yarden Y, et al. Sensitivity of mature Erbb2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J Biol Chem 2001;276:3702-8.
    • (2001) J Biol Chem , vol.276 , pp. 3702-3708
    • Xu, W.1    Mimnaugh, E.2    Rosser, M.F.3    Nicchitta, C.4    Marcu, M.5    Yarden, Y.6
  • 18
    • 0028786332 scopus 로고
    • Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • Schulte TW, Blagosklonny MV, Ingui C, Neckers L. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J Biol Chem 1995;270:24585-8.
    • (1995) J Biol Chem , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 19
    • 0033863883 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome
    • An WG, Schulte TW, Neckers LM. The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome. Cell Growth Differ 2000;11:355-60.
    • (2000) Cell Growth Differ , vol.11 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 20
    • 0141925960 scopus 로고    scopus 로고
    • FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases
    • Yao Q, Nishiuchi R, Li Q, Kumar AR, Hudson WA, Kersey JH. FLT3 expressing leukemias are selectively sensitive to inhibitors of the molecular chaperone heat shock protein 90 through destabilization of signal transduction-associated kinases. Clin Cancer Res 2003;9:4483-93.
    • (2003) Clin Cancer Res , vol.9 , pp. 4483-4493
    • Yao, Q.1    Nishiuchi, R.2    Li, Q.3    Kumar, A.R.4    Hudson, W.A.5    Kersey, J.H.6
  • 21
    • 1642541150 scopus 로고    scopus 로고
    • 17-Allylamino-17-demethoxygeldanamycin (17-AAG) is effective in down-regulating mutated, constitutively activated KIT protein in human mast cells
    • Fumo G, Akin C, Metcalfe DD, Neckers L. 17-Allylamino-17-demethoxygeldanamycin (17-AAG) is effective in down-regulating mutated, constitutively activated KIT protein in human mast cells. Blood 2004;103:1078-84.
    • (2004) Blood , vol.103 , pp. 1078-1084
    • Fumo, G.1    Akin, C.2    Metcalfe, D.D.3    Neckers, L.4
  • 22
    • 0036091221 scopus 로고    scopus 로고
    • 17-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts
    • Solit DB, Zheng FF, Drobnjak M, Munster PN, Higgins B, Verbel D, et al. 17-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts. Clin Cancer Res 2002;8:986-93.
    • (2002) Clin Cancer Res , vol.8 , pp. 986-993
    • Solit, D.B.1    Zheng, F.F.2    Drobnjak, M.3    Munster, P.N.4    Higgins, B.5    Verbel, D.6
  • 23
    • 0032484127 scopus 로고    scopus 로고
    • The assembly of progesterone receptor-hsp90 complexes using purified proteins
    • Kosano H, Stensgard B, Charlesworth MC, McMahon N, Toft D. The assembly of progesterone receptor-hsp90 complexes using purified proteins. J Biol Chem 1998;273:32973-9.
    • (1998) J Biol Chem , vol.273 , pp. 32973-32979
    • Kosano, H.1    Stensgard, B.2    Charlesworth, M.C.3    McMahon, N.4    Toft, D.5
  • 24
    • 33751111683 scopus 로고    scopus 로고
    • Hsp90 inhibition results in autophagy-mediated proteasome-independent degradation of IkappaB kinase (IKK)
    • Qing G, Yan P, Xiao G. Hsp90 inhibition results in autophagy-mediated proteasome-independent degradation of IkappaB kinase (IKK). Cell Res 2006;16:895-901.
    • (2006) Cell Res , vol.16 , pp. 895-901
    • Qing, G.1    Yan, P.2    Xiao, G.3
  • 25
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway
    • Isaacs JS, Jung YJ, Mimnaugh EG, Martinez A, Cuttitta F, Neckers LM. Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway. J Biol Chem 2002;277:29936-44.
    • (2002) J Biol Chem , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1    Jung, Y.J.2    Mimnaugh, E.G.3    Martinez, A.4    Cuttitta, F.5    Neckers, L.M.6
  • 27
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P, Rosen N. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 2002;277:39858-66.
    • (2002) J Biol Chem , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 29
    • 70350135441 scopus 로고    scopus 로고
    • Inhibition of Hsp90 via 17-DMAG induces apoptosis in a p53-dependent manner to prevent medulloblastoma
    • Ayrault O, Godeny MD, Dillon C, Zindy F, Fitzgerald P, Roussel MF, et al. Inhibition of Hsp90 via 17-DMAG induces apoptosis in a p53-dependent manner to prevent medulloblastoma. Proc Natl Acad Sci U S A 2009;106:17037-42.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 17037-17042
    • Ayrault, O.1    Godeny, M.D.2    Dillon, C.3    Zindy, F.4    Fitzgerald, P.5    Roussel, M.F.6
  • 30
    • 77956193668 scopus 로고    scopus 로고
    • Induction of premature senescence by hsp90 inhibition in small cell lung cancer
    • Restall IJ, Lorimer IA. Induction of premature senescence by hsp90 inhibition in small cell lung cancer. PLoS ONE 2010;5:e11076.
    • (2010) PLoS ONE , vol.5
    • Restall, I.J.1    Lorimer, I.A.2
  • 31
    • 0042330311 scopus 로고    scopus 로고
    • Apoptosis, necrosis and cellular senescence: Chaperone occupancy as a potential switch
    • Soti C, Sreedhar AS, Csermely P. Apoptosis, necrosis and cellular senescence: chaperone occupancy as a potential switch. Aging Cell 2003;2:39-45.
    • (2003) Aging Cell , vol.2 , pp. 39-45
    • Soti, C.1    Sreedhar, A.S.2    Csermely, P.3
  • 32
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heatshock proteins
    • Connell P, Ballinger CA, Jiang J, Wu Y, Thompson LJ, Hohfeld J, et al. The co-chaperone CHIP regulates protein triage decisions mediated by heatshock proteins. Nat Cell Biol 2001;3:93-6.
    • (2001) Nat Cell Biol , vol.3 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6
  • 33
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: A quality-control E3 ligase collaborating with molecular chaperones
    • Murata S, Chiba T, Tanaka K. CHIP: a quality-control E3 ligase collaborating with molecular chaperones. Int J Biochem Cell Biol 2003;35:572-8.
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 572-578
    • Murata, S.1    Chiba, T.2    Tanaka, K.3
  • 35
    • 0035487104 scopus 로고    scopus 로고
    • The INK4a/ARF network in tumour suppression
    • Sherr CJ.The INK4a/ARF network in tumour suppression. Nat Rev Mol Cell Biol 2001;2:731-7.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 731-737
    • Sherr, C.J.1
  • 36
    • 84875909623 scopus 로고    scopus 로고
    • Siva1 inhibits p53 function by acting as an ARF E3 ubiquitin ligase
    • Wang X, Zha M, Zhao X, Jiang P, Du W, Tam AY, et al. Siva1 inhibits p53 function by acting as an ARF E3 ubiquitin ligase. Nat Commun 2013;4:1551.
    • (2013) Nat Commun , vol.4 , pp. 1551
    • Wang, X.1    Zha, M.2    Zhao, X.3    Jiang, P.4    Du, W.5    Tam, A.Y.6
  • 37
    • 84868618042 scopus 로고    scopus 로고
    • Nanog signaling in cancer promotes stem-like phenotype and immune evasion
    • Noh KH, Kim BW, Song KH, Cho H, Lee YH, Kim JH, et al. Nanog signaling in cancer promotes stem-like phenotype and immune evasion. J Clin Invest 2012;122:4077-93.
    • (2012) J Clin Invest , vol.122 , pp. 4077-4093
    • Noh, K.H.1    Kim, B.W.2    Song, K.H.3    Cho, H.4    Lee, Y.H.5    Kim, J.H.6
  • 38
    • 84937553660 scopus 로고    scopus 로고
    • PI3K/AKT activation induces PTEN ubiquitination and destabilization accelerating tumourigenesis
    • Lee MS, Jeong MH, Lee HW, Han HJ, Ko A, Hewitt SM, et al. PI3K/AKT activation induces PTEN ubiquitination and destabilization accelerating tumourigenesis. Nat Commun 2015;6:7769.
    • (2015) Nat Commun , vol.6 , pp. 7769
    • Lee, M.S.1    Jeong, M.H.2    Lee, H.W.3    Han, H.J.4    Ko, A.5    Hewitt, S.M.6
  • 39
    • 28844451001 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
    • Shen HY, He JC, Wang Y, Huang QY, Chen JF. Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice. J Biol Chem 2005;280:39962-9.
    • (2005) J Biol Chem , vol.280 , pp. 39962-39969
    • Shen, H.Y.1    He, J.C.2    Wang, Y.3    Huang, Q.Y.4    Chen, J.F.5
  • 40
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice JF.Chaperone-mediated autophagy. Autophagy 2007;3:295-9.
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.F.1
  • 43
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang HL, Terlecky SR, Plant CP, Dice JF. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 1989;246:382-5.
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 44
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo AM, Dice JF. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 1996;273:501-3.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 45
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes FA, Dice JF. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J Cell Sci 2001;114:2491-9.
    • (2001) J Cell Sci , vol.114 , pp. 2491-2499
    • Agarraberes, F.A.1    Dice, J.F.2
  • 46
    • 0034532302 scopus 로고    scopus 로고
    • Post-translational disruption of the delta F508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes delta F508 CFTR in the rabbit reticulocyte lysate
    • Fuller W, Cuthbert AW. Post-translational disruption of the delta F508 cystic fibrosis transmembrane conductance regulator (CFTR)-molecular chaperone complex with geldanamycin stabilizes delta F508 CFTR in the rabbit reticulocyte lysate. J Biol Chem 2000;275:37462-8.
    • (2000) J Biol Chem , vol.275 , pp. 37462-37468
    • Fuller, W.1    Cuthbert, A.W.2
  • 47
    • 0034661466 scopus 로고    scopus 로고
    • CYP2E1 degradation by in vitro reconstituted systems: Role of the molecular chaperone hsp90
    • Goasduff T, Cederbaum AI. CYP2E1 degradation by in vitro reconstituted systems: role of the molecular chaperone hsp90. Arch Biochem Bioph 2000;379:321-30.
    • (2000) Arch Biochem Bioph , vol.379 , pp. 321-330
    • Goasduff, T.1    Cederbaum, A.I.2
  • 48
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    • McClellan AJ, Scott MD, Frydman J. Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways. Cell 2005;121:739-48.
    • (2005) Cell , vol.121 , pp. 739-748
    • McClellan, A.J.1    Scott, M.D.2    Frydman, J.3
  • 49
    • 84857050136 scopus 로고    scopus 로고
    • HSP90 as a platform for the assembly of more effective cancer chemotherapy
    • Whitesell L, Lin NU. HSP90 as a platform for the assembly of more effective cancer chemotherapy. Biochim Biophys Acta 2012;1823:756-66.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 756-766
    • Whitesell, L.1    Lin, N.U.2
  • 50
    • 84933509294 scopus 로고    scopus 로고
    • Phase I/II study of HSP90 inhibitor AUY922 and erlotinib for EGFR-mutant lung cancer with acquired resistance to epidermal growth factor receptor tyrosine kinase inhibitors
    • Johnson ML, Yu HA, Hart EM, Weitner BB, Rademaker AW, Patel JD, et al. Phase I/II study of HSP90 inhibitor AUY922 and erlotinib for EGFR-mutant lung cancer with acquired resistance to epidermal growth factor receptor tyrosine kinase inhibitors. J Clin Oncol 2015;33:1666-73.
    • (2015) J Clin Oncol , vol.33 , pp. 1666-1673
    • Johnson, M.L.1    Yu, H.A.2    Hart, E.M.3    Weitner, B.B.4    Rademaker, A.W.5    Patel, J.D.6


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