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Volumn 121, Issue 1, 2003, Pages 33-42

Molecular chaperone HSP90 as a novel target for cancer chemotherapy

Author keywords

Cancer chemotherapy; Geldanamycin; HSP90; Kinase; Signal transduction

Indexed keywords

17 ALLYLAMINOGELDANAMYCIN; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CELL CYCLE PROTEIN; CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; PROTEIN KINASE; STEROID RECEPTOR; UNCLASSIFIED DRUG;

EID: 0037241732     PISSN: 00155691     EISSN: None     Source Type: Journal    
DOI: 10.1254/fpj.121.33     Document Type: Review
Times cited : (10)

References (43)
  • 1
    • 0031871783 scopus 로고    scopus 로고
    • The 90-kDa stress protein, Hsp90, is a novel molecular chaperone
    • Yahara I, Minami Y and Miyata Y: The 90-kDa stress protein, Hsp90, is a novel molecular chaperone. Ann N Y Acad Sci 851, 54-60 (1998)
    • (1998) Ann N Y Acad Sci , vol.851 , pp. 54-60
    • Yahara, I.1    Minami, Y.2    Miyata, Y.3
  • 2
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely P, Schnaider T, Soti C, Prohaszka Z and Nardai G: The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol Ther 79, 129-168 (1998)
    • (1998) Pharmacol Ther , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 3
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & Co. - A holding for folding
    • Buchner J: Hsp90 & Co. - a holding for folding. Trends Biochem Sci 24, 136-141 (1999)
    • (1999) Trends Biochem Sci , vol.24 , pp. 136-141
    • Buchner, J.1
  • 4
    • 0030901877 scopus 로고    scopus 로고
    • A molecular clamp in the crystal structure of the Nterminal domain of the yeast Hsp90 chaperone
    • Prodromou C, Roe SM, Piper PW and Pearl LH: A molecular clamp in the crystal structure of the Nterminal domain of the yeast Hsp90 chaperone. Nat Struct Biol 4, 477-482 (1997)
    • (1997) Nat Struct Biol , vol.4 , pp. 477-482
    • Prodromou, C.1    Roe, S.M.2    Piper, P.W.3    Pearl, L.H.4
  • 5
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU and Pavletich NP: Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89, 239-250 (1997)
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 8
    • 0030935063 scopus 로고    scopus 로고
    • A 50 kilodalton protein associated with raf and pp60 (v-src) protein kinases is a mammalian homolog of the cell cycle control protein cdc37
    • Perdew GH, Wiegand H, Vanden Heuvel JP, Mitchell C and Singh SS: A 50 kilodalton protein associated with raf and pp60 (v-src) protein kinases is a mammalian homolog of the cell cycle control protein cdc37. Biochemistry 36, 3600-3607 (1997)
    • (1997) Biochemistry , vol.36 , pp. 3600-3607
    • Perdew, G.H.1    Wiegand, H.2    Vanden Heuvel, J.P.3    Mitchell, C.4    Singh, S.S.5
  • 9
    • 0033863883 scopus 로고    scopus 로고
    • bcr-abl and v-src proteins before their degradation by the proteasome
    • bcr-abl and v-src proteins before their degradation by the proteasome. Cell Growth Differ 11, 355-360 (2000)
    • (2000) Cell Growth Differ , vol.11 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 11
    • 0029665779 scopus 로고    scopus 로고
    • Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev 10, 1491-1502 (1996)
    • (1996) Genes Dev , vol.10 , pp. 1491-1502
    • Stepanova, L.1    Leng, X.2    Parker, S.B.3    Harper, J.W.4
  • 13
    • 0029838168 scopus 로고    scopus 로고
    • Physical interaction of mammalian CDC37 with CDK4
    • Dai K, Kobayashi R and Beach D: Physical interaction of mammalian CDC37 with CDK4. J Biol Chem 271, 22030-22034 (1996)
    • (1996) J Biol Chem , vol.271 , pp. 22030-22034
    • Dai, K.1    Kobayashi, R.2    Beach, D.3
  • 14
    • 0033590164 scopus 로고    scopus 로고
    • Distantly related cousins of MAP kinase: Biochemical properties and possible physiological functions
    • Miyata Y and Nishida E: Distantly related cousins of MAP kinase: Biochemical properties and possible physiological functions. Biochem Biophys Res Commun 266, 291-295 (1999)
    • (1999) Biochem Biophys Res Commun , vol.266 , pp. 291-295
    • Miyata, Y.1    Nishida, E.2
  • 15
    • 0032997006 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel member of the MAP kinase superfamily
    • Miyata Y, Akashi M and Nishida E: Molecular cloning and characterization of a novel member of the MAP kinase superfamily. Genes Cells 4, 299-309 (1999)
    • (1999) Genes Cells , vol.4 , pp. 299-309
    • Miyata, Y.1    Akashi, M.2    Nishida, E.3
  • 17
    • 0035877701 scopus 로고    scopus 로고
    • Specific association of a set of molecular chaperones including HSP90 and Cdc37 with MOK, a member of the MAP kinase superfamily
    • Miyata Y, Ikawa Y, Shibuya M and Nishida E: Specific association of a set of molecular chaperones including HSP90 and Cdc37 with MOK, a member of the MAP kinase superfamily. J Biol Chem 276, 21841-21848 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 21841-21848
    • Miyata, Y.1    Ikawa, Y.2    Shibuya, M.3    Nishida, E.4
  • 18
    • 0031306770 scopus 로고    scopus 로고
    • Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation
    • Pinna LA and Meggio F: Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation. Prog Cell Cycle Res 3, 77-97 (1997)
    • (1997) Prog Cell Cycle Res , vol.3 , pp. 77-97
    • Pinna, L.A.1    Meggio, F.2
  • 19
    • 0026669310 scopus 로고
    • The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
    • Miyata Y and Yahara I: The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J Biol Chem 267, 7042-7047 (1992)
    • (1992) J Biol Chem , vol.267 , pp. 7042-7047
    • Miyata, Y.1    Yahara, I.2
  • 20
    • 0029063877 scopus 로고
    • Interaction between casein kinase II and the 90-kDa stress protein, HSP90
    • Miyata Y and Yahara I: Interaction between casein kinase II and the 90-kDa stress protein, HSP90. Biochemistry 34, 8123-8129 (1995)
    • (1995) Biochemistry , vol.34 , pp. 8123-8129
    • Miyata, Y.1    Yahara, I.2
  • 21
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato S, Fujita N and Tsuruo T: Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci USA 97, 10832-10837 (2000)
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 22
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with Hsp90 and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P and Rosen N: Akt forms an intracellular complex with Hsp90 and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 277, 39858-39866 (2002)
    • (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
  • 23
    • 0033778278 scopus 로고    scopus 로고
    • Mutations in the Plk gene lead to instability of Plk protein in human tumour cell lines
    • Shimizu S and Osada H: Mutations in the Plk gene lead to instability of Plk protein in human tumour cell lines. Nat Cell Biol 2, 852-854 (2000)
    • (2000) Nat Cell Biol , vol.2 , pp. 852-854
    • Shimizu, S.1    Osada, H.2
  • 24
    • 0035355510 scopus 로고    scopus 로고
    • Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability
    • De Carcer G, Do Carmo Avides M, Lallena MJ, Glover DM and Gonzalez C: Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability. EMBO J 20, 2878-2884 (2001)
    • (2001) EMBO J , vol.20 , pp. 2878-2884
    • De Carcer, G.1    Do Carmo Avides, M.2    Lallena, M.J.3    Glover, D.M.4    Gonzalez, C.5
  • 25
    • 0034653849 scopus 로고    scopus 로고
    • Hsp 90 is a core centrosomal component and is required at different stages of the centrosome cycle in Drosophila and vertebrates
    • Lange BM, Bachi A, Wilm M and Gonzalez C: Hsp 90 is a core centrosomal component and is required at different stages of the centrosome cycle in Drosophila and vertebrates. EMBO J 19, 1252-1262 (2000)
    • (2000) EMBO J , vol.19 , pp. 1252-1262
    • Lange, B.M.1    Bachi, A.2    Wilm, M.3    Gonzalez, C.4
  • 27
    • 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 and Neckers L: Sensitivity of mature ErbB2 to geldanamycin is conferred by its kinase domain and is mediated by the chaperone protein Hsp90. J Biol Chem 276, 3702-3708 (2001)
    • (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    Neckers, L.7
  • 29
    • 0028064940 scopus 로고
    • v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 91, 8324-8328 (1994)
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 30
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW and Pearl LH: Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90, 65-75 (1997)
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 31
    • 0036219609 scopus 로고    scopus 로고
    • Hsp90 inhibotors as novel cancer chemotherapeutic agents
    • Neckers L: Hsp90 inhibotors as novel cancer chemotherapeutic agents. Trends Mol Med 8, S55-S61 (2002)
    • (2002) Trends Mol Med , vol.8
    • Neckers, L.1
  • 32
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Maloney A and Workman P: HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Expert Opin Biol Ther 2, 3-24 (2002)
    • (2002) Expert Opin Biol Ther , vol.2 , pp. 3-24
    • Maloney, A.1    Workman, P.2
  • 33
    • 0028589101 scopus 로고
    • A role for Hsp90 in cell cycle control: Wee 1 tyrosine kinase activity requires interaction with Hsp90
    • Aligue R, Akhavan-Niak H and Russell P: A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90. EMBO J 13, 6099-6106 (1994)
    • (1994) EMBO J , vol.13 , pp. 6099-6106
    • Aligue, R.1    Akhavan-Niak, H.2    Russell, P.3
  • 34
    • 0029760873 scopus 로고    scopus 로고
    • A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock
    • Chen CF, Chen Y, Dai K, Chen PL, Riley DJ and Lee WH: A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock. Mol Cell Biol 16, 4691-4699 (1996)
    • (1996) Mol Cell Biol , vol.16 , pp. 4691-4699
    • Chen, C.F.1    Chen, Y.2    Dai, K.3    Chen, P.L.4    Riley, D.J.5    Lee, W.H.6
  • 35
    • 0031909866 scopus 로고    scopus 로고
    • The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent
    • Whitesell L, Sutphin PD, Pulcini EJ, Martinez JD and Cook PH: The physical association of multiple molecular chaperone proteins with mutant p53 is altered by geldanamycin, an hsp90-binding agent. Mol Cell Biol 18, 1517-1524 (1998)
    • (1998) Mol Cell Biol , vol.18 , pp. 1517-1524
    • Whitesell, L.1    Sutphin, P.D.2    Pulcini, E.J.3    Martinez, J.D.4    Cook, P.H.5
  • 36
    • 15844363948 scopus 로고    scopus 로고
    • Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell
    • Sepehrnia B, Paz IB, Dasgupta G and Momand J: Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell. J Biol Chem 271, 15084-15090 (1996)
    • (1996) J Biol Chem , vol.271 , pp. 15084-15090
    • Sepehrnia, B.1    Paz, I.B.2    Dasgupta, G.3    Momand, J.4
  • 37
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90
    • Blagosklonny MV, Toretsky J, Bohen S and Neckers L: Mutant conformation of p53 translated in vitro or in vivo requires functional HSP90. Proc Natl Acad Sci USA 93, 8379-8383 (1996)
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 38
    • 0023766565 scopus 로고
    • Evidence that the 90-kilodalton heat shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells
    • Sanchez ER, Redmond T, Scherrer LC, Bresnick EH, Welsh MJ and Pratt WB: Evidence that the 90-kilodalton heat shock protein is associated with tubulin-containing complexes in L cell cytosol and in intact PtK cells. Mol Endocrinol 2, 756-760 (1988)
    • (1988) Mol Endocrinol , vol.2 , pp. 756-760
    • Sanchez, E.R.1    Redmond, T.2    Scherrer, L.C.3    Bresnick, E.H.4    Welsh, M.J.5    Pratt, W.B.6
  • 39
    • 0032544543 scopus 로고    scopus 로고
    • Heat-shock protein 90 (hsp90) binds in vitro to tubulin dimer and inhibits microtubule formation
    • Garnier C, Barbier P, Gilli R, Lopez C, Peyrot V and Briand C: Heat-shock protein 90 (hsp90) binds in vitro to tubulin dimer and inhibits microtubule formation. Biochem Biophys Res Commun 250, 414-419 (1998)
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 414-419
    • Garnier, C.1    Barbier, P.2    Gilli, R.3    Lopez, C.4    Peyrot, V.5    Briand, C.6
  • 40
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of Hsp90 function results in degradation of the death domain kinase, receptor-interactin protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kB activation
    • Lewis J, Devin A, Miller A, Lin Y, Rodriguez Y, Neckers L and Liu Z-G: Disruption of Hsp90 function results in degradation of the death domain kinase, receptor-interactin protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kB activation. J Biol Chem 275, 10519-10526 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3    Lin, Y.4    Rodriguez, Y.5    Neckers, L.6    Liu, Z.-G.7
  • 41
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90
    • Chen G, Cao P and Goeddel DV: TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol Cell 9, 401-410 (2002)
    • (2002) Mol Cell , vol.9 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 42
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford SL and Lindquist S: Hsp90 as a capacitor for morphological evolution. Nature 396, 336-342 (1998)
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 43
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • Queitsch C, Sangster TA and Lindquist S: Hsp90 as a capacitor of phenotypic variation. Nature 417, 598-599 (2002)
    • (2002) Nature , vol.417 , pp. 598-599
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3


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