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Volumn 13, Issue 2, 1993, Pages 869-876

Identification of a 60-Kilodalton Stress-Related Protein, p60, Which Interacts with hsp90 and hsp70

Author keywords

[No Author keywords available]

Indexed keywords

AVES; ORYCTOLAGUS CUNICULUS; SIMIAE; SIMIAN VIRUS; SIMIAN VIRUS 40;

EID: 0027439595     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.13.2.869     Document Type: Article
Times cited : (248)

References (54)
  • 1
    • 0026343040 scopus 로고
    • Biological role and regulation of the universally conserved heat shock proteins
    • Ang, D., K. Liberek, D. Skowyra, M. Zylicz, and C. Georgopoulos. 1991. Biological role and regulation of the universally conserved heat shock proteins. J. Biol. Chem. 266:24233-24236.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24233-24236
    • Ang, D.1    Liberek, K.2    Skowyra, D.3    Zylicz, M.4    Georgopoulos, C.5
  • 2
    • 0025303147 scopus 로고
    • Interaction of hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckman, R. P., L. A. Mizzen, and W. J. Welch. 1990. Interaction of hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science 248:850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckman, R.P.1    Mizzen, L.A.2    Welch, W.J.3
  • 3
    • 0024567048 scopus 로고
    • Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor
    • Bresnick, E. H., F. C. Dalman, E. R. Sanchez, and W. B. Pratt. 1989. Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor. J. Biol. Chem. 264:4992-4997.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4992-4997
    • Bresnick, E.H.1    Dalman, F.C.2    Sanchez, E.R.3    Pratt, W.B.4
  • 4
    • 0022574582 scopus 로고
    • src with the cellular proteins pp50 and pp90
    • src with the cellular proteins pp50 and pp90. Curr. Top. Microbiol. Immunol. 123:1-22.
    • (1986) Curr. Top. Microbiol. Immunol. , vol.123 , pp. 1-22
    • Brugge, J.1
  • 5
    • 0020661643 scopus 로고
    • Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: Analysis of the turnover and distribution of this complex
    • Brugge, J., W. Yonemoto, and D. Darrow. 1983. Interaction between the Rous sarcoma virus transforming protein and two cellular phosphoproteins: analysis of the turnover and distribution of this complex. Mol. Cell. Biol. 3:9-19.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 9-19
    • Brugge, J.1    Yonemoto, W.2    Darrow, D.3
  • 8
    • 0024298706 scopus 로고
    • 70K heat shock related proteins stimulate protein translocation into microsomes
    • Chirico, W. J., M. G. Waters, and G. Blobel. 1988. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature (London) 332:805-810.
    • (1988) Nature (London) , vol.332 , pp. 805-810
    • Chirico, W.J.1    Waters, M.G.2    Blobel, G.3
  • 9
    • 0025729541 scopus 로고
    • The 90-kDa heat shock protein (hsp-90) possesses an ATP binding site and autophosphorylating activity
    • Csermely, P., and C. R. Kahn. 1991. The 90-kDa heat shock protein (hsp-90) possesses an ATP binding site and autophosphorylating activity. J. Biol. Chem. 266:4943-4950.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4943-4950
    • Csermely, P.1    Kahn, C.R.2
  • 10
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies, R. J., B. D. Koch, M. Werner-Washburne, E. A. Craig, and R. Schekman. 1988. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature (London) 332:800-805.
    • (1988) Nature (London) , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 12
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Harlow, E., and D. P. Lane. 1988. Antibodies: a laboratory manual, p. 208-211. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1988) Antibodies: A Laboratory Manual , pp. 208-211
    • Harlow, E.1    Lane, D.P.2
  • 13
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
    • Heukeshoven, J., and R. Dernick. 1985. Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 6:103-112.
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 14
    • 0020604240 scopus 로고
    • Characterization of nonactivated and activated glucocorticoid-receptor complexes from intact rat thymus cells
    • Holbrook, N. J., J. E. Bodwell, M. Jeffries, and A. Munck. 1983. Characterization of nonactivated and activated glucocorticoid-receptor complexes from intact rat thymus cells. J. Biol. Chem. 258:6477-6485.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6477-6485
    • Holbrook, N.J.1    Bodwell, J.E.2    Jeffries, M.3    Munck, A.4
  • 15
    • 0026640657 scopus 로고
    • Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1
    • Honoré, B., H. Leffers, P. Madsen, H. H. Rasmussen, J. Vanderkerckhove, and J. E. Celis. 1992. Molecular cloning and expression of a transformation-sensitive human protein containing the TPR motif and sharing identity to the stress-inducible yeast protein STI1. J. Biol. Chem. 267:8485-8491.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8485-8491
    • Honoré, B.1    Leffers, H.2    Madsen, P.3    Rasmussen, H.H.4    Vanderkerckhove, J.5    Celis, J.E.6
  • 16
    • 0018726056 scopus 로고
    • A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cells
    • Kearney, J. F., A. Radbruch, B. Liesegang, and K. Rajewsky. 1979. A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cells. J. Immunol. 123:1548.
    • (1979) J. Immunol. , vol.123 , pp. 1548
    • Kearney, J.F.1    Radbruch, A.2    Liesegang, B.3    Rajewsky, K.4
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ, and GroEL along the pathway of chaperone-mediated protein folding
    • Langer, T., C. Lu, H. Echols, J. Flanagan, M. K. Hayer, and F. U. Hartl. 1992. Successive action of DnaK, DnaJ, and GroEL along the pathway of chaperone-mediated protein folding. Nature (London) 356:683-689.
    • (1992) Nature (London) , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 23
    • 85012738669 scopus 로고
    • Analysis of autoimmune DNA antibody responses using somatic cell hybridization
    • G. J. Hammerling and J. F. Kearney (ed.), Elsevier/North-Holland, Amsterdam
    • Marion, T. N., and D. E. Briles. 1981. Analysis of autoimmune DNA antibody responses using somatic cell hybridization, p. 251-258. In G. J. Hammerling and J. F. Kearney (ed.), Monoclonal antibodies and t cell hybridomas. Elsevier/North-Holland, Amsterdam.
    • (1981) Monoclonal Antibodies and T Cell Hybridomas , pp. 251-258
    • Marion, T.N.1    Briles, D.E.2
  • 24
    • 0024468795 scopus 로고
    • Evidence for the association of the heme-regulated eIF-2α kinase with the 90-kDa heat shock protein in a rabbit reticulocyte lysate in situ
    • Matts, R. L., and R. Hurst. 1989. Evidence for the association of the heme-regulated eIF-2α kinase with the 90-kDa heat shock protein in a rabbit reticulocyte lysate in situ. J. Biol. Chem. 264:15542-15547.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15542-15547
    • Matts, R.L.1    Hurst, R.2
  • 25
    • 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 I. Yahara. 1992. 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) J. Biol. Chem. , vol.267 , pp. 7042-7047
    • Miyata, Y.1    Yahara, I.2
  • 27
    • 0024469206 scopus 로고
    • Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae
    • Nicolet, C. M., and E. A. Craig. 1989. Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae. Mol. Cell. Biol. 9:3638-3646.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3638-3646
    • Nicolet, C.M.1    Craig, E.A.2
  • 29
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 30
    • 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
  • 32
    • 0022386726 scopus 로고
    • Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and species
    • Riehl, R. M., W. P. Sullivan, B. T. Vroman, V. J. Bauer, G. R. Pearson, and D. O. Toft. 1985. Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and species. Biochemistry 24:6586-6591.
    • (1985) Biochemistry , vol.24 , pp. 6586-6591
    • Riehl, R.M.1    Sullivan, W.P.2    Vroman, B.T.3    Bauer, V.J.4    Pearson, G.R.5    Toft, D.O.6
  • 33
    • 0023661048 scopus 로고
    • The 90-kilodalton peptide of the heme-regulated eIF-2α kinase has sequence similarity with the 90-kilodalton heat shock protein
    • Rose, D. W., R. E. H. Wettenhall, W. Kudlicki, G. Kramer, and B. Hardesty. 1987. The 90-kilodalton peptide of the heme-regulated eIF-2α kinase has sequence similarity with the 90-kilodalton heat shock protein. Biochemistry 26:6583-6587.
    • (1987) Biochemistry , vol.26 , pp. 6583-6587
    • Rose, D.W.1    Wettenhall, R.E.H.2    Kudlicki, W.3    Kramer, G.4    Hardesty, B.5
  • 34
    • 0024456399 scopus 로고
    • Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
    • Rothman, J. E. 1989. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell 59:591-601.
    • (1989) Cell , vol.59 , pp. 591-601
    • Rothman, J.E.1
  • 35
    • 0025605444 scopus 로고
    • Hsp56: A novel heat shock protein associated with untransformed steroid receptor complexes
    • Sanchez, E. R. 1990. Hsp56: a novel heat shock protein associated with untransformed steroid receptor complexes. J. Biol. Chem. 265:22067-22070.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22067-22070
    • Sanchez, E.R.1
  • 36
    • 0025290187 scopus 로고
    • The 56-59 kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins
    • Sanchez, E. R., L. E. Faber, W. J. Henzel, and W. B. Pratt. 1990. The 56-59 kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins. Biochemistry 29:5145-5152.
    • (1990) Biochemistry , vol.29 , pp. 5145-5152
    • Sanchez, E.R.1    Faber, L.E.2    Henzel, W.J.3    Pratt, W.B.4
  • 37
    • 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, E. R., T. Redmond, L. C. Scherrer, E. H. Bresnick, M. J. Welsh, and W. B. Pratt. 1988. 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) 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
  • 38
    • 0022342203 scopus 로고
    • Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein
    • Sanchez, E. R., D. O. Toft, M. J. Schlesinger, and W. B. Pratt. 1985. Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein. J. Biol. Chem. 260:12398-12401.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12398-12401
    • Sanchez, E.R.1    Toft, D.O.2    Schlesinger, M.J.3    Pratt, W.B.4
  • 39
    • 0023472472 scopus 로고
    • Tricine-sodium dodecylsulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa
    • Schagger, H., and G. von Jagow. 1987. Tricine-sodium dodecylsulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 40
    • 0025644194 scopus 로고
    • Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex
    • Scherrer, L. C., F. C. Dalman, E. Massa, S. Meshinchi, and W. B. Pratt. 1990. Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex. J. Biol. Chem. 265: 21397-21400.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21397-21400
    • Scherrer, L.C.1    Dalman, F.C.2    Massa, E.3    Meshinchi, S.4    Pratt, W.B.5
  • 42
    • 0025159176 scopus 로고
    • A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis
    • Sikorski, R. S., M. S. Boguski, M. Goebl, and P. Hieter. 1990. A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis. Cell 60:307-317.
    • (1990) Cell , vol.60 , pp. 307-317
    • Sikorski, R.S.1    Boguski, M.S.2    Goebl, M.3    Hieter, P.4
  • 43
    • 0025233648 scopus 로고
    • Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins
    • Smith, D. F., L. E. Faber, and D. O. Toft. 1990. Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins. J. Biol. Chem. 265:3996-4003.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3996-4003
    • Smith, D.F.1    Faber, L.E.2    Toft, D.O.3
  • 44
    • 0025640051 scopus 로고
    • Reconstitution of progesterone receptor with heat shock proteins
    • Smith, D. F., D. B. Schowalter, S. L. Kost, and D. O. Toft. 1990. Reconstitution of progesterone receptor with heat shock proteins. Mol. Endocrinol. 4:1704-1711.
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1704-1711
    • Smith, D.F.1    Schowalter, D.B.2    Kost, S.L.3    Toft, D.O.4
  • 45
    • 0026543821 scopus 로고
    • Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events
    • Smith, D. F., B. A. Stensgard, W. J. Welch, and D. O. Toft. 1992. Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events. J. Biol. Chem. 267:1350-1356.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1350-1356
    • Smith, D.F.1    Stensgard, B.A.2    Welch, W.J.3    Toft, D.O.4
  • 47
    • 0022397561 scopus 로고
    • Isolation of steroid receptor binding protein from chicken oviduct and production of monoclonal antibodies
    • Sullivan, W. P., B. T. Vroman, V. J. Bauer, R. K. Puri, R. M. Riehl, G. R. Pearson, and D. O. Toft. 1985. Isolation of steroid receptor binding protein from chicken oviduct and production of monoclonal antibodies. Biochemistry 24:4214-4222.
    • (1985) Biochemistry , vol.24 , pp. 4214-4222
    • Sullivan, W.P.1    Vroman, B.T.2    Bauer, V.J.3    Puri, R.K.4    Riehl, R.M.5    Pearson, G.R.6    Toft, D.O.7
  • 48
    • 0026710278 scopus 로고
    • Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex
    • Tai, P.-K. K., M. W. Albers, H. Chang, L. E. Faber, and S. L. Schreiber. 1992. Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex. Science 256:1315-1318.
    • (1992) Science , vol.256 , pp. 1315-1318
    • Tai, P.-K.K.1    Albers, M.W.2    Chang, H.3    Faber, L.E.4    Schreiber, S.L.5
  • 49
    • 0022427782 scopus 로고
    • The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles
    • Ungewickell, E. 1985. The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles. EMBO J. 4:3385-3391.
    • (1985) EMBO J. , vol.4 , pp. 3385-3391
    • Ungewickell, E.1
  • 50
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D., and U. I. Flügge. 1984. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138:141-143.
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 54
    • 0024077833 scopus 로고
    • Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes
    • Zimmerman, R., M. Sagstetter, M. J. Lewis, and H. R. B. Pelham. 1988. Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes. EMBO J. 7:2875-2880.
    • (1988) EMBO J. , vol.7 , pp. 2875-2880
    • Zimmerman, R.1    Sagstetter, M.2    Lewis, M.J.3    Pelham, H.R.B.4


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