메뉴 건너뛰기




Volumn 63, Issue 15, 2003, Pages 4614-4619

Cdc37 enhances proliferation and is necessary for normal human prostate epithelial cell survival

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; CELL CYCLE PROTEIN 37; CHAPERONE; CYCLIN D1; CYCLIN DEPENDENT KINASE 4; HEAT SHOCK PROTEIN 70; PROTEIN P16; RAF PROTEIN; RAF1 PROTEIN; UNCLASSIFIED DRUG;

EID: 0042635840     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (44)

References (42)
  • 1
    • 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, T. M., Finegold, M., Thompson, T. C., and Harper, J. W. Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia. Oncogene, 19: 2186-2193, 2000.
    • (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
  • 2
    • 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, E. V., and Harper, J. W. 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.
    • (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
  • 5
    • 0030839830 scopus 로고    scopus 로고
    • Analysis of mammalian Cdc37, a protein kinase targeting subunit of heat shock protein 90
    • Stepanova, L., Leng, X., and Harper, J. W. Analysis of mammalian Cdc37, a protein kinase targeting subunit of heat shock protein 90. Methods Enzymol., 283: 220-229, 1997.
    • (1997) Methods Enzymol. , vol.283 , pp. 220-229
    • Stepanova, L.1    Leng, X.2    Harper, J.W.3
  • 6
    • 0034720777 scopus 로고    scopus 로고
    • p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules
    • Hartson, S. D., Irwin, A. D., Shao, J., Scroggins, B. T., Volk, L., Huang, W., and Matts, R. L. p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules. Biochemistry, 39: 7631-7644, 2000.
    • (2000) Biochemistry , vol.39 , pp. 7631-7644
    • Hartson, S.D.1    Irwin, A.D.2    Shao, J.3    Scroggins, B.T.4    Volk, L.5    Huang, W.6    Matts, R.L.7
  • 8
    • 0035808455 scopus 로고    scopus 로고
    • Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase
    • Shao, J., Grammatikakis, N., Scroggins, B. T., Uma, S., Huang, W., Chen, J. J., Hartson, S. D., and Matts, R. L. Hsp90 regulates p50(cdc37) function during the biogenesis of the active conformation of the heme-regulated eIF2 alpha kinase. J. Biol. Chem., 276: 206-214, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 206-214
    • Shao, J.1    Grammatikakis, N.2    Scroggins, B.T.3    Uma, S.4    Huang, W.5    Chen, J.J.6    Hartson, S.D.7    Matts, R.L.8
  • 9
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., and Neckers, L. M. Inhibition of heat shock protein HSP90-pp60v-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
  • 10
    • 0029665779 scopus 로고    scopus 로고
    • Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
    • Stepanova, L., Leng, X., Parker, S. B., and Harper, J. W. Mammalian p50Cdc37 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
  • 11
    • 0029658298 scopus 로고    scopus 로고
    • CDC37 is required for p60v-src activity in yeast
    • Dey, B., Lightbody, J. J., and Boschelli, F. CDC37 is required for p60v-src activity in yeast. Mol. Biol. Cell, 7: 1405-1417, 1996.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1405-1417
    • Dey, B.1    Lightbody, J.J.2    Boschelli, F.3
  • 12
    • 0043197275 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with Hsp90 and Cdc37 and is destabilized by inhibitors of Hsp90 functiom
    • Basso, A. D., Solit, D. B., 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 functiom. J. Biol. Chem., 9: 9, 2002.
    • (2002) J. Biol. Chem. , vol.9 , pp. 9
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 13
    • 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, D. M., and Caplan, A. J. Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor. J. Biol. Chem., 276: 5814-5820, 2001.
    • (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
  • 14
    • 0344671608 scopus 로고    scopus 로고
    • Functions of the retinoblastoma protein
    • Kaelin, W. G., Jr. Functions of the retinoblastoma protein. Bioessays, 21: 950-958, 1999.
    • (1999) Bioessays , vol.21 , pp. 950-958
    • Kaelin W.G., Jr.1
  • 15
    • 0029033861 scopus 로고
    • The retinoblastoma protein and cell cycle control
    • Weinberg, R. A. The retinoblastoma protein and cell cycle control. Cell, 81: 323-330, 1995.
    • (1995) Cell , vol.81 , pp. 323-330
    • Weinberg, R.A.1
  • 17
    • 0035803395 scopus 로고    scopus 로고
    • Wide spectrum of tumors in knock-in mice carrying a Cdk4 protein insensitive to INK4 inhibitors
    • Sotillo, R., Dubus, P., Martin, J., de la Cueva, E., Ortega, S., Malumbres, M., and Barbacid, M. Wide spectrum of tumors in knock-in mice carrying a Cdk4 protein insensitive to INK4 inhibitors. EMBO J., 20: 6637-6647, 2001.
    • (2001) EMBO J. , vol.20 , pp. 6637-6647
    • Sotillo, R.1    Dubus, P.2    Martin, J.3    De la Cueva, E.4    Ortega, S.5    Malumbres, M.6    Barbacid, M.7
  • 18
    • 0028917954 scopus 로고
    • Regulation of Ras-mediated signalling: More than one way to skin a cat
    • Burgering, B. M., and Bos, J. L. Regulation of Ras-mediated signalling: more than one way to skin a cat. Trends Biochem. Sci., 20: 18-22, 1995.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 18-22
    • Burgering, B.M.1    Bos, J.L.2
  • 19
    • 0036684674 scopus 로고    scopus 로고
    • Untying the regulation of the Raf-1 kinase
    • Dhillon, A. S., and Kolch, W. Untying the regulation of the Raf-1 kinase. Arch. Biochem. Biophys., 404: 3-9, 2002.
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 3-9
    • Dhillon, A.S.1    Kolch, W.2
  • 20
    • 0029006126 scopus 로고
    • Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation
    • Marais, R., Light, Y., Paterson, H. F., and Marshall, C. J. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J., 14: 3136-3145, 1995.
    • (1995) EMBO J. , vol.14 , pp. 3136-3145
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Marshall, C.J.4
  • 21
    • 0028152333 scopus 로고
    • MAP kinase kinase kinase, MAP kinase kinase and MAP kinase
    • Marshall, C. J. MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr. Opin. Genet. Dev., 4: 82-89, 1994.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 82-89
    • Marshall, C.J.1
  • 22
    • 0029786329 scopus 로고    scopus 로고
    • Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOGMAPK pathway
    • Lavoie, J. N., L'Allemain, G., Brunet, A., Muller, R., and Pouyssegur, J. Cyclin D1 expression is regulated positively by the p42/p44MAPK and negatively by the p38/HOGMAPK pathway. J. Biol. Chem. 271: 20608-20616, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20608-20616
    • Lavoie, J.N.1    L'Allemain, G.2    Brunet, A.3    Muller, R.4    Pouyssegur, J.5
  • 23
    • 0032192153 scopus 로고    scopus 로고
    • Senescence of human fibroblasts induced by oncogenic Raf
    • Zhu, J., Woods, D., McMahon, M., and Bishop, J. M. Senescence of human fibroblasts induced by oncogenic Raf. Genes Dev., 12: 2997-3007, 1998.
    • (1998) Genes Dev. , vol.12 , pp. 2997-3007
    • Zhu, J.1    Woods, D.2    McMahon, M.3    Bishop, J.M.4
  • 24
    • 0037068753 scopus 로고    scopus 로고
    • Raf-1-induced growth arrest in human mammary epithelial cells is p16 independent and is overcome in immortal cells during conversion
    • Olsen, C. L., Gardie, B., Yaswen, P., and Stampfer, M. R. Raf-1-induced growth arrest in human mammary epithelial cells is p16 independent and is overcome in immortal cells during conversion. Oncogene, 21: 6328-6339, 2002.
    • (2002) Oncogene , vol.21 , pp. 6328-6339
    • Olsen, C.L.1    Gardie, B.2    Yaswen, P.3    Stampfer, M.R.4
  • 25
    • 0029690256 scopus 로고    scopus 로고
    • DNA methylation, molecular genetic, and linkage studies in prostate cancer
    • Jarrard, D. F., Bova, G. S., and Isaacs, W. B. DNA methylation, molecular genetic, and linkage studies in prostate cancer. Prostate Suppl., 6: 36-44, 1996.
    • (1996) Prostate Suppl. , vol.6 , pp. 36-44
    • Jarrard, D.F.1    Bova, G.S.2    Isaacs, W.B.3
  • 27
    • 0023161597 scopus 로고
    • Growth kinetics and differentiation in vitro of normal human uroepithelial cells on collagen gel substrates in defined medium
    • Reznikoff, C. A., Loretz, L. J., Pesciotta, D. M., Oberley, T. D., and Ignjatovic, M. M. Growth kinetics and differentiation in vitro of normal human uroepithelial cells on collagen gel substrates in defined medium. J. Cell. Physiol., 131: 285-301, 1987.
    • (1987) J. Cell. Physiol. , vol.131 , pp. 285-301
    • Reznikoff, C.A.1    Loretz, L.J.2    Pesciotta, D.M.3    Oberley, T.D.4    Ignjatovic, M.M.5
  • 28
    • 0027385030 scopus 로고
    • Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human raf-1 protein kinase
    • Samuels, M. L., Weber, M. J., Bishop, J. M., and McMahon, M. Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human raf-1 protein kinase. Mol. Cell. Biol., 13: 6241-6252, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6241-6252
    • Samuels, M.L.1    Weber, M.J.2    Bishop, J.M.3    McMahon, M.4
  • 30
    • 0028228616 scopus 로고
    • Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells
    • Cowley, S., Paterson, H., Kemp, P., and Marshall, C. J. Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells. Cell, 77: 841-852, 1994.
    • (1994) Cell , vol.77 , pp. 841-852
    • Cowley, S.1    Paterson, H.2    Kemp, P.3    Marshall, C.J.4
  • 31
    • 0034713329 scopus 로고    scopus 로고
    • Is beta-galactosidase staining a marker of senescence in vitro and in vivo?
    • Severino, J., Allen, R. G., Balin, S., Balin, A., and Cristofalo, V. J. Is beta-galactosidase staining a marker of senescence in vitro and in vivo? Exp. Cell Res., 257: 162-171, 2000.
    • (2000) Exp. Cell Res. , vol.257 , pp. 162-171
    • Severino, J.1    Allen, R.G.2    Balin, S.3    Balin, A.4    Cristofalo, V.J.5
  • 33
    • 0032537009 scopus 로고    scopus 로고
    • Increased cell growth and tumorigenicity in human prostate LNCaP cells by overexpression to cyclin D1
    • Chen, Y., Martinez, L. A., LaCava, M., Coghlan, L., and Conti, C. J. Increased cell growth and tumorigenicity in human prostate LNCaP cells by overexpression to cyclin D1. Oncogene, 16: 1913-1920, 1998.
    • (1998) Oncogene , vol.16 , pp. 1913-1920
    • Chen, Y.1    Martinez, L.A.2    LaCava, M.3    Coghlan, L.4    Conti, C.J.5
  • 36
    • 0036928732 scopus 로고    scopus 로고
    • Prostate stem cell antigen is a marker of late intermediate prostate epithelial cells
    • Tran, C. P., Lin, C., Yamashiro, J., and Reiter, R. E. Prostate stem cell antigen is a marker of late intermediate prostate epithelial cells. Mol. Cancer Res., 1: 113-121, 2002.
    • (2002) Mol. Cancer Res. , vol.1 , pp. 113-121
    • Tran, C.P.1    Lin, C.2    Yamashiro, J.3    Reiter, R.E.4
  • 37
    • 0036468496 scopus 로고    scopus 로고
    • Human prostate epithelial cell-type cDNA libraries and prostate expression patterns
    • Liu, A. Y., Nelson, P. S., van den Engh, G., and Hood, L. Human prostate epithelial cell-type cDNA libraries and prostate expression patterns. Prostate, 50: 92-103, 2002.
    • (2002) Prostate , vol.50 , pp. 92-103
    • Liu, A.Y.1    Nelson, P.S.2    Van den Engh, G.3    Hood, L.4
  • 41
    • 85047695528 scopus 로고    scopus 로고
    • Hsp-90-associated oncoproteins: Multiple targets of geldanamycin and its analogs
    • Blagosklonny, M. V. Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs. Leukemia (Baltimore), 16: 455-462, 2002.
    • (2002) Leukemia (Baltimore) , vol.16 , pp. 455-462
    • Blagosklonny, M.V.1
  • 42
    • 0036219609 scopus 로고    scopus 로고
    • Hsp90 inhibitors as novel cancer chemotherapeutic agents
    • Neckers, L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol. Med., 8: S55-S61, 2002.
    • (2002) Trends Mol. Med. , vol.8
    • Neckers, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.