Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 70, 2006 - Issue 6
Journal homepage
122
Views
2
CrossRef citations to date
0
Altmetric
Original Articles

Client Binding of Cdc37 Is Regulated Intramolecularly and Intermolecularly

Kazuya TERASAWADepartment of Biophysics and Biochemistry, and Undergraduate Program for Bioinformatics and Systems Biology, Graduate School of Science, The University of Tokyo
,
Fumika SHINOZAKIDepartment of Biophysics and Biochemistry, and Undergraduate Program for Bioinformatics and Systems Biology, Graduate School of Science, The University of Tokyo
,
Michiko MINAMIDepartment of Natural and Environmental Science, Faculty of Education, Tokyo Gakugei University;Department of Biochemistry and Molecular Biology, Faculty of Medicine, The University of Tokyo
&
Yasufumi MINAMIDepartment of Biophysics and Biochemistry, and Undergraduate Program for Bioinformatics and Systems Biology, Graduate School of Science, The University of Tokyo
Pages 1542-1546 | Received 10 Apr 2006, Accepted 25 Apr 2006, Published online: 22 May 2014

  • 1) Hartl, F. U., and Hayer-Hartl, M., Molecular chaperones in the cytosol: from nascent chain to folded protein. Science, 295, 1852–1858 (2002).
  • 2) Mosser, D. D., and Morimoto, R. I., Molecular chaperones and the stress of oncogenesis. Oncogene, 23, 2907–2918 (2004).
  • 3) Young, J. C., Moarefi, I., and Hartl, F. U., Hsp90: a specialized but essential protein-folding tool. J. Cell. Biol., 154, 267–273 (2001).
  • 4) Picard, D., Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci., 59, 1640–1648 (2002).
  • 5) Pratt, W. B., and Toft, D. O., Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med., 228, 111–133 (2003).
  • 6) Wegele, H., Müller, L., and Buchner, J., Hsp70 and Hsp90—a relay team for protein folding. Rev. Physiol. Biochem. Pharmacol., 151, 1–44 (2004).
  • 7) Terasawa, K., Minami, M., and Minami, Y., Constantly updated knowledge of Hsp90. J. Biochem., 137, 443–447 (2005).
  • 8) Hunter, T., and Poon, R. Y. C., Cdc37: a protein kinase chaperone? Trends Cell Biol., 7, 157–161 (1997).
  • 9) Pearl, L. H., Hsp90 and Cdc37—a chaperone cancer conspiracy. Curr. Opin. Genet. Dev., 15, 55–61 (2005).
  • 10) Brugge, J. S., Interaction of the Rous sarcoma virus protein pp60src with the cellular proteins pp50 and pp90. Curr. Top. Microbiol. Immunol., 123, 1–22 (1986).
  • 11) Stancato, L. F., Chow, Y.-H., Hutchison, K. A., Perdew, G. H., Jove, R., and Pratt, W. B., 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).
  • 12) Prince, T., Sun, L., and Matts, R. L., Cdk2: a genuine protein kinase client of Hsp90 and Cdc37. Biochemistry, 44, 15287–15295 (2005).
  • 13) Dai, K., Kobayashi, R., and Beach, D., Physical interaction of mammalian CDC37 with CDK4. J. Biol. Chem., 271, 22030–22034 (1996).
  • 14) Basso, A. D., Solit, D. B., Chiosis, G., Giri, B., Tsichlis, P., and Rosen, N., Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J. Biol. Chem., 277, 39858–39866 (2002).
  • 15) Terasawa, K., Yoshimatsu, K., Iemura, S., Natsume, T., Tanaka, K., and Minami, Y., Cdc37 iteracts with the glycine-rich loop of Hsp90 client kinases. Mol. Cell. Biol., 26, 3378–3389 (2006).
  • 16) Terasawa, K., and Minami, Y., A client-binding site of Cdc37. FEBS J., 272, 4684–4690 (2005).
  • 17) Zhao, Q., Boschelli, F., Caplan, A. J., and Arndt, K. T., Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4. J. Biol. Chem., 279, 12560–12564 (2004).
  • 18) Prince, T., and Matts, R. L., Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37. J. Biol. Chem., 279, 39975–39981 (2004).
  • 19) Silverstein, A. M., Grammatikakis, N., Cochran, B. H., Chinkers, M., and Pratt, W. B., p50cdc37 binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site. J. Biol. Chem., 273, 20090–20095 (1998).
  • 20) Grammatikakis, N., Lin, J.-H., Grammatikakis, A., Tsichlis, P. N., and Cochran, B. H., p50cdc37 acting in concert with Hsp90 is required for Raf-1 function. Mol. Cell. Biol., 19, 1661–1672 (1999).
  • 21) Hartson, S. D., Irwin, A. D., Shao, J., Scroggins, B. T., Volk, L., Huang, W., and Matts, R. L., p50cdc37 is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules. Biochemistry, 39, 7631–7644 (2000).
  • 22) Roe, S. M., Ali, M. M. U., Meyer, P., Vaughan, C. K., Panaretou, B., Piper, P. W., Prodromou, C., and Pearl, L. H., The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50cdc37. Cell, 116, 87–98 (2004).
  • 23) Shao, J., Irwin, A., Hartson, S. D., and Matts, R. L., Functional dissection of Cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding. Biochemistry, 42, 12577–12588 (2003).
  • 24) Cutforth, T., and Rubin, G. M., Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell, 77, 1027–1036 (1994).
  • 25) Bandhakavi, S., McCann, R. O., Hanna, D. H., and Glover, C. V. C., A positive feedback loop between protein kinase CKII and Cdc37 promotes the activity of multiple protein kinases. J. Biol. Chem., 278, 2829–2836 (2003).
  • 26) Hanks, S. K., and Hunter, T., The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J., 9, 576–596 (1995).
  • 27) Zhang, W., Hirshberg, M., McLaughlin, S. H., Lazer, G. A., Grossmann, J. G., Nielsen, P. R., Sobott, F., Robinson, C. V., Jackson, S. E., and Laue, E. D., Biochemical and structural studies of the interaction of Cdc37 with Hsp90. J. Mol. Biol., 340, 891–907 (2004).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.