Cdc37 is a molecular chaperone with specific functions in signal transduction

Genes and Development

Volumn 11, Issue 14, 1997, Pages 1775-1785

  Kimura, Yoko ^a   Rutherford, Suzanne L ^a   Miyata, Yoshihiko ^b   Yahara, Ichiro ^b   Freeman, Brian C ^c   Yue, Lin ^a   Morimoto, Richard I ^c   Lindquist, Susan ^a  

^a UNIVERSITY OF CHICAGO   (United States)

^b TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE   (Japan)

^c NORTHWESTERN UNIVERSITY   (United States)

Author keywords

Cdc37; Chaperone; Hsp90; Kinase; Signal transduction

Indexed keywords

CASEIN KINASE; CELL CYCLE PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 90;

ARTICLE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SUBUNIT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DETERMINATION; SIGNAL TRANSDUCTION;

EID: 0030745769     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.11.14.1775     Document Type: Article

References (50)

1. Bohen, S.P. and K.R. Yamamoto. 1994. Modulation of steroid receptor signal transduction by heat shock proteins. In The biology of heat shock proteins and molecular chaperones (ed. R. Morimoto, A. Tissieres, and C. Georgopoulos), pp. 313-334, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
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. Bose, S., T. Weikl, H. Bugl, and J. Buchner. 1996. Chaperone function of Hsp90-associated proteins. Science 274: 1715-1717.
4. Brugge, J.S. 1986. Interaction of the Rous sarcoma virus protein pp60src with the cellular proteins pp50 and pp90. Curr. Top. Microbiol. Immunol. 123: 1-22.
5. Brugge, J.S., E. Erikson, and R.L. Erikson. 1981. The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteins. Cell 25: 363-372.
6. Chang, H.-C., D.F. Nathan, and S. Lindquist. 1997. In vivo analysis of the Hsp90 cochaperone Stil (p60). Mol. Cell Biol. 17: 318-325.
7. Chang, H.-C. and S. Lindquist. 1994. Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae. J. Biol. Chem. 269: 24983-24988.
8. Cutforth, T. and G.M. Ruhin. 1994. Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 77: 1027-1036.
9. Dai, K., R. Kobayashi, and D. Beach. 1996. Physical interaction of mammalian CDC37 with CDK4. J. Biol. Chem. 271: 22030-22034.
10. v-src activity in yeast. Mol. Biol. Cell 7: 1405-1417.
11. Dickson, BJ., A. van der Strafen, M. Dominguez, and E. Hafen. 1996. Mutations modulating raf signaling in Drosophila eye development. Genetics 142: 163-171.
12. Dougherty, J.J., D.A. Rabideau, A.M. Iannotti, W.P. Sullivan, and D.O. Toft. 1987. Identification of the 90 kDa substrate of rat liver type II casein kinase with the heat shock protein which binds steroid receptors. Biochim. Biophys. Acta 927: 74-80.
13. Duina, A.A., H.-C.J. Chang, J.A. Marsh, S. Lindquist, and R.F. Garber. 1996. A cyclophilin function in Hsp90-dependent signal transduction. Science 274: 1713-1715.
14. Ellis, J. 1987. Proteins as molecular chaperones. Nature 328: 378-379.
15. 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.
16. Freeman, B.C. and R.I. Morimoto. 1996. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of non-native protein and protein refolding. EMBO J. 15: 2969-2979.
17. Freeman, B.C., D.O. Toft, and R.I. Morimoto. 1996. Molecular chaperone machines: Chaperone activities of the cyclophilin CYP-40 and the steroid aporeceptor associated protein, p23. Science 274: 1718-1720.
18. Georgopoulos, C. and WJ. Welch. 1993. Role of the major heat shock proteins as molecular chaperones. In Annu. Rev. Cell Biol. (ed. G. E. Palade), pp. 601-634.
19. 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.
20. Hanks, S.K. and T. Hunter. 1995. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification. FASEB J. 9: 576-596.
21. 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.
22. Jakob, U. and J. Buchner. 1994. Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem. Sci. 19: 205-211.
23. 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.
24. Jones, E. 1991. Tackling the protease: A problem in Saccharomyces cerevisiae. Methods Enzymol. 194: 428-453.
25. 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.
26. Lindsley, D.L. and G.G. Zimm. 1992. The genome of Drosophila melanogaster. Academic Press, New York, NY.
27. McCann, R. and C.V.C. Glover. 1995. Evidence for the physiological interaction of yeast Cdc37 and casein kinase II. Mol. Biol. Cell (Supp.) 6: 133a.
28. Mclnick, J., J.L. Dul, and Y. Argon. 1994. Sequential interaction of the chaperones BiP and GRP94 with immunoglobin chains in the endoplasmic reticulum. Nature 370: 373-375.
29. 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.
30. _. 1995. Interaction between casein kinase II and the 90-kDa stress protein, HSP90. Biochemistry 34: 8123-8129.
31. Nair, S.C., E.J. Toran, R.A. Rimerman, S. Hjermstad, T.E. Smithgall, and D.F. Smith. 1996. 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 1: 237-250.
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. 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 348: 166-168.
34. Reed, S.I. 1980. The selection of S. cerevisiae mutants defective in the start event of cell division. Genetics 95: 561-577.
35. Reed, S.I., M.A. de Barros Lopes, J. Freemason, J.A. Hadwiger, J.Y. Ho, R. Horwitz, C.A. Jones, A.T. Lorincz, M.D. Mendenhall, T.A. Peterson, S.L. Richardson, and C. Wittenberg. 1985. Genetic and molecular analysis of division control in yeast. Cold Spring Harbor Symp. Quant. Biol. 50: 627-634.
36. Rutherford, S.L. and C.S. Zuker. 1994. Protein folding and the regulation of signaling pathways. Cell 79: 1129-1132.
37. Schroder, H.T., T. Langer, F.-U. Hartl, and B. Bukau. 1993. DnaK, DnaJ, GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12: 4137-4144.
38. Schutz, A.R., T.H. Giddings, Jr., E. Steiner, and M. Winey. 1997. The yeast CDC37 gene interacts with MPSI and is required for proper execution of spindle pole body duplication. J. Cell Biol. 136: 969-982.
39. Shaknovich, R., G. Shue, and D.S. Kohtz. 1992. Conformational activation of a basic helix-loop-helix protein (MyoDI) by the C-terminal region of marine HSP90 [HSP84). Mol. Cell Biol. 12: 5059-5068.
40. Sikorski, R.S. and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharormyces cerivisiae. Genetics 122: 19-27.
41. Smith, D.S. 1993. Dynamics of heat shock protein 90-progester-one receptor binding and the disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 7: 1418-1429.
42. Smith, D.S. and D.O. Toft. 1993. Steroid receptors and their associated proteins. Mol. Endocrinol. 7: 4-11.
43. Stancato, L.F., Y.H. Chow, K.A. Hutison, 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.
44. Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes & Dev. 10: 1491-1502.
45. Wartmann, M. and RJ. Davis. 1994. The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. J. Biol. Chem. 269: 6695-6701.
46. Whitelaw, M.L., K. Hutchison, and G.H. Perdew. 1991. A 50-kDa cytosolic protein complexed with the 90-kDa heat shock protein (hsp90) is the same protein complexed with v-Src hsp90 in cells transformed by the Rous sarcoma virus. J. Biol. Chem. 266: 16436-16440.
47. Wiech, H., J. Buchner, R. Zimmermann, and U. Jakob. 1992. Hsp90 chaperones protein folding in vitro. Nature 358: 169-170.
48. Wohlwill, A.D. and J.J. Bonner. 1991. Genetic analysis of chromosome region 63 of Drosophila melanogaster. Genetics 128: 763-775.
49. Xu, Y. and S. Lindquist. 1993. Heat-shock protein hsp90 governs the activity of v-Src kinase. Proc. Natl. Acad. Sci. 90: 7074-7078.
50. Ziemiecki, A., M.G. Catelli, I. Joab, and B. Moncharmont. 1986. Association of the heat shock protein hsp90 with steroid hormone receptors and tyrosine kinase oncogcne products. Biochem. Biophys. Res. Commun. 138: 1298-1307.