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Volumn 10, Issue 12, 1996, Pages 1491-1502

Mammalian p50(Cdc37) is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

Author keywords

Cyclin dependent kinase; D type cyclin; Hsp90; molecular chaperone; p50(Cdc37)

Indexed keywords

CHAPERONE; COMPLEMENTARY DNA; CYCLIN DEPENDENT KINASE; CYCLINE; HEAT SHOCK PROTEIN 90; PROTEIN SUBUNIT; CDC37 PROTEIN, HUMAN; CDC37 PROTEIN, MOUSE; CDC37 PROTEIN, S CEREVISIAE; CDK4 PROTEIN, HUMAN; CDK4 PROTEIN, MOUSE; CELL CYCLE PROTEIN; CHAPERONIN; CYCLIN D; CYCLIN DEPENDENT KINASE 4; DROSOPHILA PROTEIN; ONCOPROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 0029665779     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.10.12.1491     Document Type: Article
Times cited : (454)

References (48)
  • 1
    • 0028589101 scopus 로고
    • A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90
    • Aligue, R., H. Akhavan-Niak, and P. Russell. 1994. A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90. EMBO J. 13: 6099-6106.
    • (1994) EMBO J. , vol.13 , pp. 6099-6106
    • Aligue, R.1    Akhavan-Niak, H.2    Russell, P.3
  • 3
    • 0028999582 scopus 로고
    • Hold'em and Fold'em: Chaperones and signal transduction
    • Bohen, S.P., A. Kralli, and K.R. Yamamoto. 1995. Hold'em and Fold'em: Chaperones and signal transduction. Science 268:1303-1304.
    • (1995) Science , vol.268 , pp. 1303-1304
    • Bohen, S.P.1    Kralli, A.2    Yamamoto, K.R.3
  • 4
    • 0027337893 scopus 로고
    • Expression of pp60v-src in Saccharomyces cerevisiae results in elevation of p34CDC28 kinase activity and release of the dependence of DNA replication on mitosis
    • Boschelli, F. 1993. Expression of pp60v-src in Saccharomyces cerevisiae results in elevation of p34CDC28 kinase activity and release of the dependence of DNA replication on mitosis. Mol. Cell. Biol. 13: 5112-5121.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5112-5121
    • Boschelli, F.1
  • 5
    • 0022574582 scopus 로고
    • Interaction of the Rous sarcoma virus protein pp60v-src with the cellular proteins p50 and p90
    • Brugge, J.S. 1986. Interaction of the Rous sarcoma virus protein pp60v-src with the cellular proteins p50 and p90. Curr. Top. Microbiol. Immunol. 123: 1-22.
    • (1986) Curr. Top. Microbiol. Immunol. , vol.123 , pp. 1-22
    • Brugge, J.S.1
  • 6
    • 0019444479 scopus 로고
    • The specific interaction of Rous sarcoma virus transforming protein, pp60src, with two cellular proteins
    • Brugge, J.S., E. Erikson, and R.L. Erickson. 1981. The specific interaction of Rous sarcoma virus transforming protein, pp60src, with two cellular proteins. Cell 25: 363-372.
    • (1981) Cell , vol.25 , pp. 363-372
    • Brugge, J.S.1    Erikson, E.2    Erickson, R.L.3
  • 7
    • 0028135173 scopus 로고
    • Cdc2 regulatory factors
    • Coleman, T.R. and W.G. Dunphy. 1994. Cdc2 regulatory factors. Curr. Biol. 6: 877-882.
    • (1994) Curr. Biol. , vol.6 , pp. 877-882
    • Coleman, T.R.1    Dunphy, W.G.2
  • 8
    • 0027532449 scopus 로고
    • Phosphorylation independent activation of human cyclin-dependent kinase 2 by cyclin A in vitro
    • Connell-Crowley, L., M.J. Solomon, N. Wei, and J.W. Harper. 1993. Phosphorylation independent activation of human cyclin-dependent kinase 2 by cyclin A in vitro. Mol. Biol. Cell 4: 79-92.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 79-92
    • Connell-Crowley, L.1    Solomon, M.J.2    Wei, N.3    Harper, J.W.4
  • 9
    • 0028363670 scopus 로고
    • Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila
    • Cutforth, T. and G.M. Rubin. 1994. Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 77: 1027-1036.
    • (1994) Cell , vol.77 , pp. 1027-1036
    • Cutforth, T.1    Rubin, G.M.2
  • 10
    • 0027083108 scopus 로고
    • Activation of human cyclin-dependent kinases in vitro
    • Desai, D., Y. Gu, and D.O. Morgan. 1992. Activation of human cyclin-dependent kinases in vitro. Mol. Biol. Cell 3: 571-582.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 571-582
    • Desai, D.1    Gu, Y.2    Morgan, D.O.3
  • 11
    • 0030040989 scopus 로고    scopus 로고
    • The YDJ1 molecular chaperone facilitates formation of active p60v-src in yeast
    • Dey, B., A.J. Caplan, and F. Boschelli. 1996. The YDJ1 molecular chaperone facilitates formation of active p60v-src in yeast. Mol. Biol. Cell 7: 91-100.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 91-100
    • Dey, B.1    Caplan, A.J.2    Boschelli, F.3
  • 12
    • 0027193228 scopus 로고
    • Torso, a receptor tyrosine kinase required for embryonic pattern formation, shares substrates with the sevenless and EGF-R pathways in Drosophila
    • Doyle, H.J. and J.M. Bishop. 1993. Torso, a receptor tyrosine kinase required for embryonic pattern formation, shares substrates with the sevenless and EGF-R pathways in Drosophila. Genes & Dev. 7: 633-646.
    • (1993) Genes & Dev. , vol.7 , pp. 633-646
    • Doyle, H.J.1    Bishop, J.M.2
  • 14
    • 0026552630 scopus 로고
    • CDK2 encodes a 33 kDa cyclin A-associated protein kinase and is expressed before CDC2 in the cell cycle
    • Elledge, S.J., R. Richman, F. Hall, R. Williams, N. Logsdon, and J.W. Harper. 1992. CDK2 encodes a 33 kDa cyclin A-associated protein kinase and is expressed before CDC2 in the cell cycle. Proc. Natl. Acad. Sci. 89: 2907-2911.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 2907-2911
    • Elledge, S.J.1    Richman, R.2    Hall, F.3    Williams, R.4    Logsdon, N.5    Harper, J.W.6
  • 15
    • 0023057566 scopus 로고
    • Nucleotide sequence of the yeast cell division cycle start genes CDC28, CDC36, CDC37, and CDC39, and a structural analysis of the predicted products
    • Ferguson, J., J.Y. Ho, T.A. Peterson, and S.I. Reed. 1986. Nucleotide sequence of the yeast cell division cycle start genes CDC28, CDC36, CDC37, and CDC39, and a structural analysis of the predicted products. Nucleic Acids Res. 14: 6681-6697.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 6681-6697
    • Ferguson, J.1    Ho, J.Y.2    Peterson, T.A.3    Reed, S.I.4
  • 16
    • 0028807103 scopus 로고
    • Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase
    • Fisher, R.P., P. Jin, H.M. Chamberlin, and D.O. Morgan. 1995. Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase. Cell 83: 47-57.
    • (1995) Cell , vol.83 , pp. 47-57
    • Fisher, R.P.1    Jin, P.2    Chamberlin, H.M.3    Morgan, D.O.4
  • 17
    • 0029017132 scopus 로고
    • Cdc37 is required for association of the protein kinase Cdc28 with G1 and mitotic cyclins
    • Gerber, M.R., A. Farrell, R.J. Deshaies, I. Herskowitz, and D.O. Morgan. 1995. Cdc37 is required for association of the protein kinase Cdc28 with G1 and mitotic cyclins. Proc. Natl. Acad. Sci. 92: 4651-4655.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 4651-4655
    • Gerber, M.R.1    Farrell, A.2    Deshaies, R.J.3    Herskowitz, I.4    Morgan, D.O.5
  • 18
  • 20
    • 0028023828 scopus 로고
    • Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function
    • Hartson, S.D. and R.L. Matts. 1994. Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function. Biochemistry 33: 8912-8920.
    • (1994) Biochemistry , vol.33 , pp. 8912-8920
    • Hartson, S.D.1    Matts, R.L.2
  • 21
    • 0027938209 scopus 로고
    • Cyclins and cancer II: Cyclin D and CDK inhibitors come of age
    • Hunter, T. and J. Pines. 1994. Cyclins and cancer II: Cyclin D and CDK inhibitors come of age. Cell 79: 573-582.
    • (1994) Cell , vol.79 , pp. 573-582
    • Hunter, T.1    Pines, J.2
  • 22
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • Hunter, T. and B. Sefton. 1980. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc. Natl. Acad. Sci. 77: 1311-1315.
    • (1980) Proc. Natl. Acad. Sci. , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.2
  • 23
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones
    • Jakob, U. and J. Buchner. 1994. Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem. Sci. 19: 205-211.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 24
    • 0029026540 scopus 로고
    • Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways
    • Kimura, Y., I. Yahara, and S. Lindquist. 1995. Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268: 1362-1365.
    • (1995) Science , vol.268 , pp. 1362-1365
    • Kimura, Y.1    Yahara, I.2    Lindquist, S.3
  • 25
    • 0028080878 scopus 로고
    • Suppression of cyclin-dependent kinase 4 during induced differentiation of erythroleukemia cells
    • Kiyokawa, H., V.M. Richon, R.A. Rifkind, and P.A. Marks. 1994. Suppression of cyclin-dependent kinase 4 during induced differentiation of erythroleukemia cells. Mol. Cell. Biol. 14: 7195-7203.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7195-7203
    • Kiyokawa, H.1    Richon, V.M.2    Rifkind, R.A.3    Marks, P.A.4
  • 27
    • 0028181760 scopus 로고
    • Identification of G1 kinase activity for Cdk6, a novel cyclin D partner
    • Meyerson, M. and E. Harlow. 1994. Identification of G1 kinase activity for Cdk6, a novel cyclin D partner. Mol. Cell. Biol. 14: 2077-2086.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2077-2086
    • Meyerson, M.1    Harlow, E.2
  • 28
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan, D.O. 1995. Principles of CDK regulation. Nature 374: 131-134.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 29
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: Interactions with steroid receptor and a protein kinase
    • Nathan, D.F. and S. Lindguist. 1995. Mutational analysis of Hsp90 function: Interactions with steroid receptor and a protein kinase. Mol. Cell. Biol. 15: 3917-3925.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindguist, S.2
  • 30
  • 31
    • 0019485241 scopus 로고
    • A cellular protein that associates with the transforming protein of Rous sarcoma virus is a heat shock protein
    • Opperman, H., W. Levinson, and J.M. Bishop. 1981. A cellular protein that associates with the transforming protein of Rous sarcoma virus is a heat shock protein. Proc. Natl. Acad. Sci. 78: 1067-1071.
    • (1981) Proc. Natl. Acad. Sci. , vol.78 , pp. 1067-1071
    • Opperman, H.1    Levinson, W.2    Bishop, J.M.3
  • 32
    • 0024473604 scopus 로고
    • 1 events and regulation of cell proliferation
    • 1 events and regulation of cell proliferation. Science 246: 603-608.
    • (1989) Science , vol.246 , pp. 603-608
    • Pardee, A.B.1
  • 34
    • 0025815731 scopus 로고
    • Evidence that the 90-kDa heat shock protein HSP90 exists in cytosol in heteromeric complexes containing Hsp70 and three other proteins with Mr of 63,000, 56,000, and 50,000
    • Perdew, G.H. and M.L. Whitelaw. 1991. Evidence that the 90-kDa heat shock protein HSP90 exists in cytosol in heteromeric complexes containing Hsp70 and three other proteins with Mr of 63,000, 56,000, and 50,000. J. Biol Chem. 266: 6708-6713.
    • (1991) J. Biol Chem. , vol.266 , pp. 6708-6713
    • Perdew, G.H.1    Whitelaw, M.L.2
  • 35
    • 0019162297 scopus 로고
    • The selection of S. cerevisiae mutants defective in the start event of cell division
    • Reed, S.I. 1980. The selection of S. cerevisiae mutants defective in the start event of cell division. Genetics 95: 561-577.
    • (1980) Genetics , vol.95 , pp. 561-577
    • Reed, S.I.1
  • 37
    • 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, T.W., M.V. Blagosklonny, C. Ingui, and L. Neckers. 1995. Disruption of the Raf-1-Hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J. Biol. Chem. 270: 24585-24588.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 38
    • 0028171292 scopus 로고
    • Cycling on cue
    • Sherr, C.J. 1994. Cycling on cue. Cell 75: 551-555.
    • (1994) Cell , vol.75 , pp. 551-555
    • Sherr, C.J.1
  • 41
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell free system
    • Stancato, L.F., Y.-H. Chow, K.A. Hutchison, G.H. Perdew, R. Jove, and W.B. Pratt. 1993. Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell free system. J. Biol. Chem. 268: 21711-21716.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.-H.2    Hutchison, K.A.3    Perdew, G.H.4    Jove, R.5    Pratt, W.B.6
  • 42
    • 0028882228 scopus 로고
    • In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein
    • Tassan, J.P., M. Jaquenoud, A.M. Fry, S. Frutiger, G.J. Hughes, and E.A. Nigg. 1995. In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein. EMBO J. 14: 5608-5617.
    • (1995) EMBO J. , vol.14 , pp. 5608-5617
    • Tassan, J.P.1    Jaquenoud, M.2    Fry, A.M.3    Frutiger, S.4    Hughes, G.J.5    Nigg, E.A.6
  • 43
    • 0029008667 scopus 로고
    • The KIN28 gene is required for both RNA polymerase II mediated transcription and phosphorylation of the Rpblp CTD
    • Valay, J.-G., M. Simon, M.-F. Dubois, O. Bensaude, C. Facca, and G. Faye. 1995. The KIN28 gene is required for both RNA polymerase II mediated transcription and phosphorylation of the Rpblp CTD. J. Mol. Biol. 249: 535-544.
    • (1995) J. Mol. Biol. , vol.249 , pp. 535-544
    • Valay, J.-G.1    Simon, M.2    Dubois, M.-F.3    Bensaude, O.4    Facca, C.5    Faye, G.6
  • 44
    • 0025949447 scopus 로고
    • A 50-kDa cytosolic protein complexed with the 90-kDa heat shock protein hsp90 is the same protein complexed with pp60v-src/hsp90 in cells transformed by Rous sarcoma virus
    • Whitelaw, W.L., K. Hutchison, and G.W. Perdew. 1991. A 50-kDa cytosolic protein complexed with the 90-kDa heat shock protein hsp90 is the same protein complexed with pp60v-src/hsp90 in cells transformed by Rous sarcoma virus. J. Biol. Chem. 266: 16436-16440.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16436-16440
    • Whitelaw, W.L.1    Hutchison, K.2    Perdew, G.W.3
  • 45
    • 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
    • Whitesel, L., E.G. Mimnaugh, B. De Costa, C.E. Myers, and L.N. Neckers. 1994. 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. 91: 8324-8328.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 8324-8328
    • Whitesel, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.N.5
  • 46
    • 0029033861 scopus 로고
    • The retinoblastoma protein and cell cycle control
    • Weinberg, R.A. 1995. The retinoblastoma protein and cell cycle control. Cell 81: 323-330.
    • (1995) Cell , vol.81 , pp. 323-330
    • Weinberg, R.A.1
  • 47
    • 0027291238 scopus 로고
    • Heat shock protein hsp90 governs the activity of pp60v-src kinase
    • Xu, Y. and S.L. Lindquist. 1993. Heat shock protein hsp90 governs the activity of pp60v-src kinase. Proc. Natl. Acad. Sci. 90: 7074-7078.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 7074-7078
    • Xu, Y.1    Lindquist, S.L.2
  • 48
    • 0019972369 scopus 로고
    • Inhibition of DNA synthesis in murine tumor cells by geldanamycin, an antibiotic of the benzoquinoid ansamycin group
    • Yamaki, H., H. Suzuki, E.C. Choi, and N. Tanaka. 1982. Inhibition of DNA synthesis in murine tumor cells by geldanamycin, an antibiotic of the benzoquinoid ansamycin group. J. Antibiot. 35: 886-892.
    • (1982) J. Antibiot. , vol.35 , pp. 886-892
    • Yamaki, H.1    Suzuki, H.2    Choi, E.C.3    Tanaka, N.4


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