CDC37 is required for p60(v-src) activity in yeast

Molecular Biology of the Cell

Volumn 7, Issue 9, 1996, Pages 1405-1417

  Dey, Barna ^a,b   Lightbody, James J ^a   Boschelli, Frank ^a  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NATIONAL INSTITUTE OF DENTAL AND CRANIOFACIAL RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL CYCLE PROTEIN; CHAPERONE; DETERGENT; FUNGAL PROTEIN; HEAT SHOCK PROTEIN 90; HYDROXYUREA; PROTEIN KINASE P60; DODECYL SULFATE SODIUM; DROSOPHILA PROTEIN; TYROSINE; UREA;

ARTICLE; CELL CYCLE PHASE; CELL SYNCHRONIZATION; CELL VIABILITY; ENZYME ACTIVITY; EXTRACT; FUNGUS MUTANT; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SOLUBILIZATION; TEMPERATURE SENSITIVE MUTANT; YEAST; CELL CYCLE G1 PHASE; CELL CYCLE G2 PHASE; CHEMISTRY; ENZYME ACTIVATION; GENE EXPRESSION REGULATION; GENETICS; LETHAL GENE; METABOLISM; MITOSIS; MUTATION; PHOSPHORYLATION; SOLUBILITY; SUPPRESSOR GENE; TEMPERATURE;

FUNGI;

CELL CYCLE PROTEINS; DROSOPHILA PROTEINS; ENZYME ACTIVATION; G1 PHASE; G2 PHASE; GENE EXPRESSION REGULATION, FUNGAL; GENES, LETHAL; GENES, SUPPRESSOR; MITOSIS; MOLECULAR CHAPERONES; MUTATION; ONCOGENE PROTEIN PP60(V-SRC); PHOSPHORYLATION; SODIUM DODECYL SULFATE; SOLUBILITY; TEMPERATURE; TYROSINE; UREA; YEASTS;

EID: 0029658298     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.7.9.1405     Document Type: Article

References (66)

1. 1-ATPase. Proc. Natl. Acad. Sci. USA 87, 4986-4990.
2. Aligue, R., Akhavan-Niak, H., and Russell, P. (1994). A role for Hsp90 in cell-cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90. EMBO J. 13, 6099-6106.
3. Becker, D.M., Guarente, L., Guthrie, C., and Fink, G.R. (1991). High-efficiency transformation of yeast by electroporation. Methods Enzymol. 194, 182-187.
4. Boeke, J.D., Lacroute, F., and Fink, G.R. (1984). A positive selection for mutants lacking orotidine 5′-phosphate decarboxylase activity in yeast: 5-fluoroorotic acid resistance. Mol. Gen. Genet. 181, 288-291.
5. Bohen, S.P., and Yamamoto, K.R. (1994). Modulation of steroid receptor signal transduction by heat shock proteins. In: The Biology of Heat Shock Proteins and Molecular Chaperones, ed. R.I. Morimoto, A. Tissereres, and C. Georgopoulos, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 313-334.
6. CDC28 kinase is dependent on the integrity of the SH2 domain. J. Cell Sci. 105, 519-528.
7. Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
8. Bresnick, E.H., Dalman, F.C., Sanchez, E.R., and Pratt, W.B. (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.
9. src with the cellular proteins pp50 and pp90. Curr. Top. Microbiol. Immunol. 123, 1-22.
10. src, with two cellular proteins. Cell 25, 363-372.
11. v-src in Saccharomyces cerevisiae cells. Mol. Cell. Biol. 7, 2180-2187.
12. Burr, J.G., Dreyfuss, G., Penman, S., and Buchanan, J.M. (1980). Association of the src gene product of Rous sarcoma virus with cytoskeletal structures of chicken embryo fibroblasts. Proc. Natl. Acad. Sci. USA 77, 3484-3488.
13. Caplan, A.J., and Douglas, M.G. (1991). Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J. Cell Biol. 114, 609-621.
14. v-src to the plasma membrane. Proc. Natl. Acad. Sci. USA 79, 7117-7121.
15. Craig, E.A., Baxter, B.K., Becker, J., Halladay, J., and Ziegelhoffer, T. (1994). Cytosolic Hp70s of Saccharomyces cerevisiae: roles in protein synthesis, protein translocation, proteolysis, and regulation. In: The Biology of Heat-Shock Proteins and Molecular Chaperones, ed. R.I. Morimoto, A. Tissieres, and C. Georgopoulos. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 31-52.
16. Craig, E.A., Gambill, B.D., and Nelson, R.J. (1993). Heat-shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57, 402-414.
17. src myristylation and membrane association and for cell transformation. Mol. Cell. Biol. 4, 1834-1842.
18. Cutforth, T., and Rubin, G.M. (1994). Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 77, 1027-1036.
19. Cyr, D.M. (1995). Cooperation of the molecular chaperone YDJ1 with specific Hsp70 homologs to suppress protein aggregation. FEBS Lett. 359, 129-132.
20. Cyr, D.M., and Douglas, M.G. (1994). Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue YDJ1. J. Biol. Chem. 269, 9798-9804.
21. Cyr, D.M., Langer, T., and Douglas, M.G. (1994). DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 19, 176-181.
22. v-src-mediated Lethality and Cell-Cycle Progression in Yeast. Ph.D. Thesis. Detroit, MI: Wayne State University.
23. v-src in yeast. Mol. Biol. Cell 7, 91-100.
24. Feaver, W.J., Svejstrup, J.Q., Henry, N.L., and Kornberg, R.D. (1994). Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK. Cell 79, 1103-1109.
25. Ferguson, J., Ho, J.-Y., Peterson, T., and Reed, S.I. (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.
26. v-src expressed in the yeast Saccharomyces cerevisiae. Mol. Biol. Cell 5, 283-296.
27. Forsburg, S.L., and Nurse, P. (1991). Cell-cycle regulation in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Annu. Rev. Cell Biol. 7, 227-256.
28. v-src prevent association with the detergent-insoluble cellular matrix. Mol. Cell. Biol. 11, 1207-1213.
29. 1 and mitotic cyclins. Proc. Natl. Acad. Sci. USA 92, 4651-4655.
30. Grammatikakis, N., Grammatikakis, A., Yoneda, M., Yu, Q., Banerjee, S.D., and Toole, B.P. (1995). A novel glycosaminoglycan-binding protein is the vertebrate homologue of the cell-cycle control protein, Cdc37. J. Biol. Chem. 270, 16198-16205.
31. src with Triton X-100-resistant cellular structure correlates with morphological transformation. Proc. Natl. Acad. Sci. USA 84, 2312-2316.
32. Hayes, S.A., and Dice, J.F. (1996). Roles of molecular chaperones in protein degradation. J. Cell Biol. 132, 255-258.
33. src, Hsp90, and p50 in a cell-free system. J. Biol. Chem. 267, 2902-2908.
34. Itoh, H., Fukuda, Y., Murata, K., and Kimura, A. (1983). Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
35. Johnson, J.L., and Toft, D.O. (1994). A novel chaperone complex for steroid receptors involving heat-shock proteins, immunophilins, and p23. J. Biol. Chem. 269, 24989-24993.
36. v-src mutants that induce different cell transformation parameters. J. Virol. 60, 849-857.
37. Jove, R., and Hanafusa, H. (1987). Cell transformation by the viral src gene. Annu. Rev. Cell Biol. 3, 31-56.
38. Kilmartin, J.V. and Adams, A.E.M. (1984). Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces. J. Cell Biol. 98, 922-933.
39. Kimura, Y., Yahara, I., and Lindquist, S. (1995). Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science 268, 1362-1365.
40. Kohrer, K., and Domdey, H. (1991). Preparation of high molecular weight RNA. Methods Enzymol. 194, 398-405.
41. src proteins expressed in yeast. Proc. Natl. Acad. Sci. USA 84, 4455-4459.
42. v-src fails to phosphorylate proteins of 115-120 kDa in chicken embryo fibroblasts. Proc. Natl. Acad. Sci. USA 85, 2608-2612.
43. v-src and other viral protein-tyrosine kinases. J. Virol. 61, 2420-2427.
44. Matt, R.L., and Hurst, R. (1989). Evidence for the association of the heme-regulated eIF-2α kinase with the 90-kDa heat-shock protein in rabbit reticulocyte lysate in situ. J. Biol. Chem. 264, 15542-15547.
45. Mitraki, A., and King, J. (1989). Protein folding intermediates and inclusion body formation. Biotechnology 7, 690-697.
46. Miyata, Y., and Yahara, I. (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, 7042-7057.
47. Nathan, D.F., and Lindquist, S. (1995). Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15, 3917-3925.
48. Oppermann, H., Levison, W., and Bishop, J.M. (1981). A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein. Proc. Natl. Acad. Sci. USA 78, 1067-1071.
49. Parsell, D.A., Kowal, A.S., Singer, M.A., and Lindquist, S. (1994). Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372, 475-478.
50. Parsell, D.A., and Lindquist, S. (1993). The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27, 437-496.
51. 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.
52. Reed, S.I. (1980). The selection of S. cerevisiae mutants defective in the start event of cell division. Genetics 95, 561-577.
53. Reed, S.I., et al. (1985). Genetic and molecular analysis of division control in yeast. Cold Spring Harbor Symp. Quant. Biol. 50, 627-634.
54. c-src molecules. J. Cell Biol. 100, 409-418.
55. Rose, D.W., Welch, W.J., Kramer, G., and Hardesty, B. (1989). Possible involvement of the 90-kDa heat-shock protein in the regulation of protein synthesis. J. Biol. Chem. 264, 6239-6244.
56. Rose, M., Novick, P., Thomas, J., Botstein, D., and Fink, G. (1987). A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene 60, 237-243.
57. Scherrer, L.C., Dalman, F.C., Massa, E., Meshinchi, S., and Pratt, W.B. (1990). Structural and functional reconstitution of the glucocorticoid receptor-Hsp90 complex. J. Biol. Chem. 265, 21397-21400.
58. Sherman, F., Fink, G.R., and Hicks, J.B. (1986). Methods in Yeast Genetics: A Laboratory Manual, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
59. Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
60. Smith, D.F. (1993). Dynamics of heat-shock protein 90-progesterone receptor binding and the disactivation loop model for steroid receptor complexes. Mol. Endocrinol. 7, 1418-1429.
61. Stancato, L.F., Chow, Y.-H., Hutchison, K.A., Perdew, G.H., Jove, R., and Pratt, W.B. (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.
62. Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. Genes Dev. 10, 1491-1502.
63. Strathmann, M., Hamilton, B.A., Mayeda, C.A., Simon, M.I., Meyerowitz, E.M., and Palazzolo, M.J. (1991). Transposon-facilitated DNA sequencing. Proc. Natl. Acad. Sci. USA 88, 1247-1250.
64. Valay, J.-G., Simon, M., Dubois, M.-F., Bensaude, O., Facca, C., and Faye, G. (1995). The KIN28 gene is required both for RNA polymerase II-mediated transcription and phosphorylation of the Rbplp CTD. J. Mol. Biol. 249, 535-544.
65. v-src do not phosphorylate cellular proteins of 120-150 kDa. Oncogene 4, 231-236.
66. v-src kinase. Proc. Natl. Acad. Sci. USA 90, 7074-7078.