메뉴 건너뛰기




Volumn 78, Issue , 2015, Pages 103-112

Cdc37 as a co-chaperone to Hsp90

Author keywords

Cancer; Cdc37; Hsp90; Protein kinase

Indexed keywords

CDC37 PROTEIN, HUMAN; CELL CYCLE PROTEIN; CHAPERONIN; HEAT SHOCK PROTEIN 90; PROTEIN AGGREGATE;

EID: 84930207925     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-319-11731-7_5     Document Type: Article
Times cited : (49)

References (42)
  • 1
    • 84879478480 scopus 로고    scopus 로고
    • Targeting the PI3K/Akt/mTOR pathway in castration-resistant prostate cancer
    • Bitting RL, Armstrong AJ (2013) Targeting the PI3K/Akt/mTOR pathway in castration-resistant prostate cancer. Endocr Relat Cancer 20:83–99
    • (2013) Endocr Relat Cancer , vol.20 , pp. 83-99
    • Bitting, R.L.1    Armstrong, A.J.2
  • 2
    • 1642569697 scopus 로고    scopus 로고
    • DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity
    • Boellmann F, Guettouche T, Guo Y, Fenna M, Mnayer L, Voellmy R (2004) DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity. Proc Natl Acad Sci U S A 101:4100–4105
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4100-4105
    • Boellmann, F.1    Guettouche, T.2    Guo, Y.3    Fenna, M.4    Mnayer, L.5    Voellmy, R.6
  • 3
    • 84899668980 scopus 로고    scopus 로고
    • Molecular cochaperones: Tumor growth and cancer treatment
    • Calderwood SK (2013) Molecular cochaperones: tumor growth and cancer treatment. Scientifica 2013:217513
    • (2013) Scientifica , vol.2013
    • Calderwood, S.K.1
  • 4
    • 84857509287 scopus 로고    scopus 로고
    • Molecular chaperones in mammary cancer growth and breast tumor therapy
    • Calderwood SK, Gong J (2012) Molecular chaperones in mammary cancer growth and breast tumor therapy. J Cell Biochem 113:1096–1103
    • (2012) J Cell Biochem , vol.113 , pp. 1096-1103
    • Calderwood, S.K.1    Gong, J.2
  • 6
    • 70349507340 scopus 로고    scopus 로고
    • The shock of aging: Molecular chaperones and the heat shock response in longevity and aging-a mini-review
    • Calderwood SK, Murshid A, Prince T (2009) The shock of aging: molecular chaperones and the heat shock response in longevity and aging-a mini-review. Gerontology 55:550–558
    • (2009) Gerontology , vol.55 , pp. 550-558
    • Calderwood, S.K.1    Murshid, A.2    Prince, T.3
  • 7
    • 38149116851 scopus 로고    scopus 로고
    • Multiple kinases and system robustness: A link between Cdc37 and genome integrity
    • Caplan AJ, Ma’ayan A, Willis IM (2007a) Multiple kinases and system robustness: a link between Cdc37 and genome integrity. Cell Cycle 6:3145–3147
    • (2007) Cell Cycle , vol.6 , pp. 3145-3147
    • Caplan, A.J.1    Ma’Ayan, A.2    Willis, I.M.3
  • 8
    • 33846651282 scopus 로고    scopus 로고
    • Molecular chaperones and protein kinase quality control
    • Caplan AJ, Mandal AK, Theodoraki MA (2007b) Molecular chaperones and protein kinase quality control. Trends Cell Biol 17:87–92
    • (2007) Trends Cell Biol , vol.17 , pp. 87-92
    • Caplan, A.J.1    Mandal, A.K.2    Theodoraki, M.A.3
  • 9
    • 21744445069 scopus 로고    scopus 로고
    • Heat shock proteins in cancer: Diagnostic, prognostic, predictive, and treatment implications
    • Ciocca DR, Calderwood SK (2005) Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones 10:86–103
    • (2005) Cell Stress Chaperones , vol.10 , pp. 86-103
    • Ciocca, D.R.1    Calderwood, S.K.2
  • 10
    • 84872358363 scopus 로고    scopus 로고
    • Heat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: An update
    • Ciocca DR, Arrigo AP, Calderwood SK (2013) Heat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an update. Arch Toxicol 87:19–48
    • (2013) Arch Toxicol , vol.87 , pp. 19-48
    • Ciocca, D.R.1    Arrigo, A.P.2    Calderwood, S.K.3
  • 11
    • 80054756986 scopus 로고    scopus 로고
    • The role of p23, Hop, immunophilins, and other co-chaperones in regulating Hsp90 function
    • Cox MB, Johnson JL (2011) The role of p23, Hop, immunophilins, and other co-chaperones in regulating Hsp90 function. Methods Mol Biol 787:45–66
    • (2011) Methods Mol Biol , vol.787 , pp. 45-66
    • Cox, M.B.1    Johnson, J.L.2
  • 12
    • 0029658298 scopus 로고    scopus 로고
    • CDC37 is required for p60v-src activity in yeast
    • Dey B, Lightbody JJ, Boschelli F (1996) CDC37 is required for p60v-src activity in yeast. Mol Biol Cell 7:1405–1417
    • (1996) Mol Biol Cell , vol.7 , pp. 1405-1417
    • Dey, B.1    Lightbody, J.J.2    Boschelli, F.3
  • 13
    • 84934438837 scopus 로고    scopus 로고
    • Protein misassembly: Macromolecular crowding and molecular chaperones
    • Ellis RJ (2007) Protein misassembly: macromolecular crowding and molecular chaperones. Adv Exp Med Biol 594:1–13
    • (2007) Adv Exp Med Biol , vol.594 , pp. 1-13
    • Ellis, R.J.1
  • 14
    • 0030659844 scopus 로고    scopus 로고
    • Differential in vivo regulation of steroid hormone receptor activation by Cdc37p
    • Fliss AE, Fang Y, Boschelli F, Caplan AJ (1997) Differential in vivo regulation of steroid hormone receptor activation by Cdc37p. Mol Biol Cell 8:2501–2509
    • (1997) Mol Biol Cell , vol.8 , pp. 2501-2509
    • Fliss, A.E.1    Fang, Y.2    Boschelli, F.3    Caplan, A.J.4
  • 15
    • 37549060720 scopus 로고    scopus 로고
    • Targeting Cdc37 inhibits multiple signalling pathways and induces growth arrest in prostate cancer cells
    • Gray PJ Jr, Stevenson MA, Calderwood SK (2007) Targeting Cdc37 inhibits multiple signalling pathways and induces growth arrest in prostate cancer cells. Cancer Res 67:11942–11950
    • (2007) Cancer Res , vol.67 , pp. 11942-11950
    • Gray, P.J.1    Stevenson, M.A.2    Calderwood, S.K.3
  • 17
    • 2342558431 scopus 로고    scopus 로고
    • Androgen receptor in prostate cancer
    • Heinlein CA, Chang C (2004) Androgen receptor in prostate cancer. Endocr Rev 25:276–308
    • (2004) Endocr Rev , vol.25 , pp. 276-308
    • Heinlein, C.A.1    Chang, C.2
  • 20
    • 38449090443 scopus 로고    scopus 로고
    • Cdc37 regulation of the kinome: When to hold’em and when to fold’em
    • Karnitz LM, Felts SJ (2007) Cdc37 regulation of the kinome: when to hold’em and when to fold’em. Sci STKE 2007:pe22
    • (2007) Sci STKE , vol.2007
    • Karnitz, L.M.1    Felts, S.J.2
  • 21
    • 0012999148 scopus 로고    scopus 로고
    • Interaction of Hsp90 with the nascent form of the mutant epidermal growth factor receptor EGFRvIII
    • Lavictoire SJ, Parolin DA, Klimowicz AC, Kelly JF, Lorimer IA (2003) Interaction of Hsp90 with the nascent form of the mutant epidermal growth factor receptor EGFRvIII. J Biol Chem 278:5292–5299
    • (2003) J Biol Chem , vol.278 , pp. 5292-5299
    • Lavictoire, S.J.1    Parolin, D.A.2    Klimowicz, A.C.3    Kelly, J.F.4    Lorimer, I.A.5
  • 22
    • 0042527167 scopus 로고    scopus 로고
    • Cdc37 goes beyond Hsp90 and kinases
    • MacLean M, Picard D (2003) Cdc37 goes beyond Hsp90 and kinases. Cell Stress Chaperones 8:114–119
    • (2003) Cell Stress Chaperones , vol.8 , pp. 114-119
    • Maclean, M.1    Picard, D.2
  • 23
    • 22344439139 scopus 로고    scopus 로고
    • CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone
    • Miyata Y, Nishida E (2005) CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone. Mol Cell Biochem 274:171–179
    • (2005) Mol Cell Biochem , vol.274 , pp. 171-179
    • Miyata, Y.1    Nishida, E.2
  • 25
    • 12344291243 scopus 로고    scopus 로고
    • Hsp90 and Cdc37- a chaperone cancer conspiracy
    • Pearl LH (2005) Hsp90 and Cdc37- a chaperone cancer conspiracy. Curr Opin Gen Dev 15:55–61
    • (2005) Curr Opin Gen Dev , vol.15 , pp. 55-61
    • Pearl, L.H.1
  • 26
    • 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, Singh SS (1997) 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) 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
  • 27
    • 0035937187 scopus 로고    scopus 로고
    • Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor
    • Rao J, Lee P, Benzeno S, Cardozo C, Albertus J, Robins DM, Caplan AJ (2001) Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor. J Biol Chem 276:5814–5820
    • (2001) J Biol Chem , vol.276 , pp. 5814-5820
    • Rao, J.1    Lee, P.2    Benzeno, S.3    Cardozo, C.4    Albertus, J.5    Robins, D.M.6    Caplan, A.J.7
  • 28
    • 0019166897 scopus 로고
    • The selection of amber mutations in genes required for completion of start, the controlling event of the cell division cycle of S. Cerevisiae
    • Reed SI (1980) The selection of amber mutations in genes required for completion of start, the controlling event of the cell division cycle of S. cerevisiae. Genetics 95:579–588
    • (1980) Genetics , vol.95 , pp. 579-588
    • Reed, S.I.1
  • 31
    • 59449107850 scopus 로고    scopus 로고
    • Targeting CDC37: An alternative, kinase-directed strategy for disruption of oncogenic chaperoning
    • Smith JR, Workman P (2009) Targeting CDC37: an alternative, kinase-directed strategy for disruption of oncogenic chaperoning. Cell Cycle 8:362–372
    • (2009) Cell Cycle , vol.8 , pp. 362-372
    • Smith, J.R.1    Workman, P.2
  • 32
    • 0034087051 scopus 로고    scopus 로고
    • The oncoprotein kinase chaperone CDC37 functions as an oncogene in mice and collaborates with both c-myc and cyclin D1 in transformation of multiple tissues
    • Stepanova L, Finegold M, DeMayo F, Schmidt EV, Harper JW (2000a) The oncoprotein kinase chaperone CDC37 functions as an oncogene in mice and collaborates with both c-myc and cyclin D1 in transformation of multiple tissues. Mol Cell Biol 20:4462–4473
    • (2000) Mol Cell Biol , vol.20 , pp. 4462-4473
    • Stepanova, L.1    Finegold, M.2    Demayo, F.3    Schmidt, E.V.4    Harper, J.W.5
  • 33
    • 0034720255 scopus 로고    scopus 로고
    • Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia
    • Stepanova L, Yang G, DeMayo F, Wheeler TM, Finegold M, Thompson TC, Harper JW (2000b) Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia. Oncogene 19:2186–2193
    • (2000) Oncogene , vol.19 , pp. 2186-2193
    • Stepanova, L.1    Yang, G.2    Demayo, F.3    Wheeler, T.M.4    Finegold, M.5    Thompson, T.C.6    Harper, J.W.7
  • 35
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: Emerging mechanistic insights
    • Taipale M, Jarosz DF, Lindquist S (2010) HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol 11:515–528
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 37
    • 23844483494 scopus 로고    scopus 로고
    • Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90
    • Turnbull EL, Martin IV, Fantes PA (2005) Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90. FEBS J 272:4129–4140
    • (2005) FEBS J , vol.272 , pp. 4129-4140
    • Turnbull, E.L.1    Martin, I.V.2    Fantes, P.A.3
  • 39
    • 84874324273 scopus 로고    scopus 로고
    • Novel interaction between the cochaperone Cdc37 and Rho GTPase exchange factor Vav3 promotes androgen receptor activity and prostate cancer growth
    • Wu F, Peacock SO, Rao S, Lemmon SK, Burnstein KL (2013) Novel interaction between the cochaperone Cdc37 and Rho GTPase exchange factor Vav3 promotes androgen receptor activity and prostate cancer growth. J Biol Cell 288:5463–5474
    • (2013) J Biol Cell , vol.288 , pp. 5463-5474
    • Wu, F.1    Peacock, S.O.2    Rao, S.3    Lemmon, S.K.4    Burnstein, K.L.5
  • 40
    • 84865213364 scopus 로고    scopus 로고
    • The double edge of the HSP90-CDC37 chaperone machinery: Opposing determinants of kinase stability and activity
    • Xu W, Neckers L (2012) The double edge of the HSP90-CDC37 chaperone machinery: opposing determinants of kinase stability and activity. Future Oncol 8:939–942
    • (2012) Future Oncol , vol.8 , pp. 939-942
    • Xu, W.1    Neckers, L.2
  • 42
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (1998) Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94:471–480
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.