In vivo analysis of the Hsp90 cochaperone Sti1 (p60)

Molecular and Cellular Biology

Volumn 17, Issue 1, 1997, Pages 318-325

  Chang, Hui Chen Jane ^a   Nathan, Debra F ^a   Lindquist, Susan ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; HEAT SHOCK PROTEIN 90;

ARTICLE; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE; VERTEBRATA;

EID: 0031013723     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.1.318     Document Type: Article

References (62)

1. Bohen, S. P., and K. R. Yamamoto. 1994. Modulation of steroid receptor signal transduction by heat shock proteins, p. 313-334. In R. I. Morimoto, A. Tissieres. and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor. N.Y.
2. Borkovich, K. A., F. W. Farrelly, D. B. Finkelstein, J. Taulien, and S. Lindquist. 1989. Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol. Cell. Biol. 9:3919-3930.
3. Bresnick, E. H., F. C. Dalman, and W. B. Pratt. 1990. Direct stoichiometric evidence that the untransformed Mr 300,000, 9S, glucocorticoid receptor is a core unit derived from a larger heteromeric complex. Biochemistry 29: 520-527.
4. 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.
5. src with the cellular proteins pp50 and pp90. Curr. Top. Microbiol. Immunol. 123:1-22.
6. Catelli, M. G., N. Binart. T. I. Jung, J. M. Renoir, E. E. Baulieu, J. R. Feramisco, and W. J. Welch. 1985. The common 90-kd protein component of non-transformed '8S' steroid receptors is a heat-shock protein. EMBO J. 4:3131-3135.
7. Chang, H.-C. J., and S. Lindquist. 1994. Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae. J. Biol. Chem. 269:24983-24988.
8. Chen. S., V. Prapapanich, R. A. Rimerman, B. Honore, and D. Smith. 1996. Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins Hsp90 and Hsp70. Mol. Endocrinol. 10:682-693.
9. Dalman. F. C., R. J. Koenig. G. H. Perdew, E. Massa, and W. B. Pratt. 1990. In contrast to the glucocorticoid receptor, the thyroid hormone receptor is translated in the DNA binding state and is not associated with hsp90. J. Biol. Chem. 265:3615-3618.
10. Dalman, F. C., L. J. Sturzenbecker, A. A. Levin, D. A. Lucas, G. H. Perdew, M. Petkovitch, P. Chambon, J. F. Grippo, and W. B. Pratt. 1991. Retinoic acid receptor belongs to a subclass of nuclear receptors that do not form "docking" complexes with hsp90. Biochemistry 30:5605-5608.
11. Denis, M., L. Poellinger, A. C. Wikstom, and J. A. Gustafsson. 1988. Requirement of hormone for thermal conversion of the glucocorticoid receptor to a DNA-binding state. Nature (London) 333:686-688.
12. Dittmar, K. D., K. A. Hutchison, J. K. Owens-Grillo, and W. B. Pratt. 1996. Reconstitution of the steroid receptor hsp90 heterocomplex assembly system of rabbit reticulocyte lysate. J. Biol. Chem. 271:12833-12839.
13. Duina, A. A., H.-C. J. Chang, J. A. Marsh, S. Lindquist, and R. F. Gaber. A cyclophilin function in Hsp90-mediated signal transduction. Science, in press.
14. Flynn, G. C., T. G. Chappell, and J. E. Rothman. 1989. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245: 385-390.
15. Freeman, B. C., and R. I. Morimoto. 1995. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein folding. EMBO J. 15:2969-2979.
16. Frydman, J., and F.-U. Hartl. 1994. Molecular chaperone functions of hsp70 and hsp60 in protein folding, p. 251-284. In R. I. Morimoto, A. Tissieres, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
17. Garabedian, M. J., and K. R. Yamamoto. 1992. Genetic dissection of the signaling domain of a mammalian steroid receptor in yeast. Mol. Biol. Cell 3:1245-1257.
18. Hutchison, K. A., M. J. Czar, L. C. Scherrer, and W. B. Pratt. 1992. Monovalent cation selectivity for ATP-dependent association of the glucocorticoid receptor with Hsp70 and Hsp90. J. Biol. Chem. 267:14047-14053.
19. Hutchison, K. A., K. D. Dittmar, and W. B. Pratt. 1994. All of the factors required for assembly of the glucocorticoid receptor into a functional heterocomplex with heat shock protein 90 are preassociated in a self-sufficient protein folding structure, a "foldosome." J. Biol. Chem. 269:27894-27899.
20. Hutchison, K. A., L. F. Stancato, J. K. Owens-Grillo, J. L. Johnson, P. Krishna, D. O. Toft, and W. B. Pratt. 1995. The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90. J. Biol. Chem. 270:18841-18847.
21. Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
22. Jakob, U., H. Lilie, I. Meyer, and J. Buchner. 1995. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. J. Biol. Chem. 270:7288-7294.
23. Kimura, Y., S. L. Rutherford, Y. Miyata, B. C. Freeman, L. Yue, R. I. Morimoto, and S. Lindquist. Submitted for publication.
24. 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.
25. Laemmli, U. K, 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
26. Mandel, M., and A. Higa. 1970. Calcium-dependent bacteriophage DNA infection. J. Mol. Biol. 53:159-162.
27. Melnick, J., J. L. Dul, and Y. Argon. 1994. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature (London) 370:373-375.
28. Mendel, D. B., and E. Orti. 1988. Isoform composition and stoichiometry of the approximately 90-kDa heat shock protein associated with glucocorticoid receptors. J. Biol. Chem. 263:6695-6702.
29. Meshinchi, S., E. R. Sanchez, K. J. Martell, and W. B. Pratt. 1990. Elimination and reconstitution of the requirement for hormone in promoting temperature-dependent transformation of cytosolic glucocorticoid receptors to the DNA-binding state. J. Biol. Chem. 265:4863-4870.
30. 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.
31. Nair, S. C., E. J. Toran, R. A. Rimerman, S. Hjermstad, T. E. Smithgall, and D. F. Smith. A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, fes tyrosine kinase, heat shock transcription factor HSF1, and the arylhydrocarbon receptor. Cell Stress Chaperones, in press.
32. Nathan, D. F., and S. Lindquist. 1995. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15:3917-3925.
33. 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.
34. Owens-Grillo, J. K., M. J. Czar, K. A. Hutchison, K. Hoffmann, G. H. Perdew, and W. B. Pratt. 1996. A model of protein targeting mediated by immunophilins and other proteins that bind to hsp90 via tetratricopeptide repeat domains. J. Biol. Chem. 271:13468-13475.
35. Picard, D., B. Khursheed, M. J. Garabedian, M. G. Fortin, S. Lindquist, and K. R. Yamamoto. 1990. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature (London) 348:166-168.
36. Prapapanich, V., S. Chen, S. C. Nair, R. A. Rimerman, and D. Smith. 1996. Molecular cloning of human p48, a transient component of progesterone receptor complexes and Hsp70-binding protein. Mol. Endocrinol. 10:420-431.
37. Pratt, W. B. 1992. Control of steroid receptor function and cytoplasmicnuclear transport by heat shock proteins. Bioessays 14:841-848.
38. Pratt, W. B. 1993. The role of heat shock proteins in regulating the function. folding, and trafficking of the glucocorticoid receptor. J. Biol. Chem. 268: 21455-21458.
39. Pratt, W. B. 1987. Transformation of glucocorticoid and progesterone receptors to the DNA-binding state. J. Cell Biochem. 35:51-68.
40. Pratt, W. B., L. C. Scherrer, K. A. Hutchison, and F. C. Dalman. 1992. A model of glucocorticoid receptor unfolding and stabilization by a heat shock protein complex. J. Steroid Biochem. Mol. Biol. 41:223-229.
41. Redeuilh, G., B. Moncharmont, C. Secco, and E. E. Baulieu. 1987. Subunit composition of the molybdate-stabilized "8-9 S" nontransformed estradiol receptor purified from calf uterus. J. Biol. Chem. 262:6969-6975.
42. Rose, D. W., R. E. Wettenhall, W. Kudlicki, G. Kramer, and B. Hardesty. 1987. The 90-kilodalton peptide of the heme-regulated eIF-2 alpha kinase has sequence similarity with the 90-kilodalton heat shock protein. Biochemistry 26:6583-6587.
43. Saccharomyces Genome Database. World Wide Web site: http://genomewww.stanford.edu/Saccharomyces/.
44. 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. 86:1123-1127.
45. Schena, M., and K. R. Yamamoto. 1988. Mammalian glucocorticoid receptor derivatives enhance transcription in yeast. Science 241:965-967.
46. Scherrer, L. C., F. C. Dalman, E. Massa, S. Meshinchi, and W. B. Pratt. 1990. Structural and functional reconstitution of the glucocorticoid receptorhsp90 complex. J. Biol. Chem. 265:21397-21400.
47. Scherrer, L. C., K. A. Hutchison, E. R. Sanchez, S. K. Randall, and W. B. Pratt. 1992. A heat shock protein complex isolated from rabbit reticulocyte lysate can reconstitute a functional glucocorticoid receptor-Hsp90 complex. Biochemistry 31:7325-7329.
48. v-src. J. Biol. Chem. 260:14292-14296,
49. Shue, G., and D. S. Kohtz. 1994. Structural and functional aspects of basic helix-loop-helix protein folding by heat-shock protein 90. J. Biol. Chem. 269:2707-2711.
50. Sikorski, R. S., and P. Hieter. 1989. A system to shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
51. Smith, D. F. 1993. Dynamics of heat shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 8:1418-1430.
52. 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.
53. Smith, D. F., D. B. Schowalter, S. L. Kost, and D. O. Toft. 1990. Reconstitution of progesterone receptor with heat shock proteins. MoI. Endocrinol. 4:1704-1711.
54. 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.
55. Smith, D. F., W. P. Sullivan, T. N. Marion, K. Zaitsu, B. Madden, D. J. McCormick, and D. O. Toft. 1993. Identification of a 60-kilodalton stressrelated protein, p60. which interacts with hsp90 and hsp70. Mol. Cell. Biol. 13:869-876.
56. Smith, D. F., and D. O. Toft. 1993. Steroid receptors and their associated proteins. Mol. Endocrinol. 7:4-11.
57. Smith, D. F., L. Whitesell, S. C. Nair, S. Chen, V. Prapapanich, and R. A. Rimerman. 1995. Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol. Cell. Biol. 15:6804-6812.
58. 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 he reconstituted in a cell-free system. J. Biol. Chem. 268:21711-21716.
59. Wartmann, M., and R. J. Davis. 1994. The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. J. Biol. Chem. 269:6695-6701.
60. Wiech, H., J. Buchner, R. Zimmermann, and U. Jakob. 1992. Hsp90 chaperones protein folding in vitro. Nature (London) 358:169-170.
61. v-src kinase. Proc. Natl. Acad. Sci. USA 90:7074-7078.
62. Yonehara, M., Y. Minami, Y. Kawata, J. Nagai, and I. Yahara. 1996. Heatinduced chaperone activity of HSP90. J. Biol. Chem. 271:2641-2645.