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Gene Review

CDC37  -  Cdc37p

Saccharomyces cerevisiae S288c

Synonyms: Cell division control protein 37, Hsp90 chaperone protein kinase-targeting subunit, Hsp90 co-chaperone Cdc37, SMO1, YD9489.03, ...
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Disease relevance of CDC37

  • These data suggest that the expression of Cdc37 may promote inappropriate proliferation and may be an important early step in the development of human prostate cancer [1].
  • Two such proteins, Cdc37p and Sup45p, when overexpressed allowed partial relief of MPA toxicity, strongly suggesting that their lower amount after MPA treatment significantly contributed to the MPA effect [2].

High impact information on CDC37

  • Our studies demonstrate that Cdc37 has a general role in kinome biogenesis [3].
  • This degradation phenotype was suppressed when cdc37 mutant cells were grown at reduced temperatures, although this did not lead to a full restoration of kinase activity [3].
  • We propose a model in which Cdc37 can function independently of Hsp90, although its ability to do so is restricted by its normally low expression levels [4].
  • The protein kinase-binding domain of Cdc37 was sufficient for yeast cell viability and permitted efficient signaling through the yeast MAP kinase-signaling pathway [4].
  • The yeast CDC37 gene interacts with MPS1 and is required for proper execution of spindle pole body duplication [5].

Biological context of CDC37

  • The genetic interaction between KIN28 and the CDC37 cell division cycle gene suggests that a connection exists between the activity of CDK-Kin28p and cell-cycle progression [6].
  • Isolation and transcriptional characterization of three genes which function at start, the controlling event of the Saccharomyces cerevisiae cell division cycle: CDC36, CDC37, and CDC39 [7].
  • The quantities calculated for the three mRNA species were low, ranging from 1.5 +/- 1 copies per haploid cell for the CDC36 mRNA to 3.1 +/- 1.5 and 4.6 +/- 2 copies per haploid cell for the CDC37 and CDC39 mRNAs, respectively [7].
  • The genes CDC36, CDC37, and CDC39, thought to function in the cell division control process in Saccharomyces cerevisiae, were isolated from a recombinant plasmid library prepared by partial digestion of S. cerevisiae genomic DNA with Sau3A and insertion into the S. cerevisiae-Escherichia coli shuttle vector YRp7 [7].
  • Since the activation pathway for p60(v-src) and steroid hormone receptors is similar, the present study analyzed the hormone-dependent transactivation by androgen receptors and glucocorticoid receptors in yeast cells expressing a mutant version of the CDC37 gene [8].

Anatomical context of CDC37

  • These data indicate that CDC37 can function as an oncogene in mice and suggests that the establishment of protein kinase pathways mediated by Cdc37-Hsp90 can be a rate-limiting event in epithelial cell transformation [9].

Associations of CDC37 with chemical compounds

  • Consistent with the existence of a recently described positive feedback loop between CK2 and Cdc37, overexpression of ZDS1,2 also suppressed the temperature sensitivity, abnormal morphology, and GA sensitivity of a CK2 phosphorylation-deficient mutant of CDC37, cdc37-S14A, as well as the GA sensitivity of a cdc37-1 allele [10].
  • Models for Cdc37p regulation of steroid hormone receptors are discussed [8].
  • CK2 phosphorylates a conserved serine residue in the N-terminal extremity of Cdc37 in vitro and in yeast as well as mammalian cells, and this is the unique phosphorylation site of Cdc37 under normal conditions [11].

Physical interactions of CDC37

  • Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase [12].
  • We found that, when separately expressed, the N-terminal lobe of Cdc28 interacted strongly with the C-terminal moiety of Cdc37 in a two-hybrid system [13].
  • Pulse-chase analysis indicates that Cdc28 and Cak1 proteins are both destabilized when Cdc37 function is absent during but not after translation [14].

Enzymatic interactions of CDC37

  • Expression of CDC37 truncation mutants that were deleted for the Hsp90-binding site stabilized v-Src and led to some folding in both sti1Delta and hsc82Delta strains [4].

Regulatory relationships of CDC37

  • In addition, Cdc37 promotes the production of Cak1, but not that of Cdc28, when coexpressed in insect cells [14].
  • Three components of the MAP kinase signalling system (Src, Raf, and Mek) exist in complexes with hsp90 and a 50-kDa protein that is the mammalian homolog of the yeast cell cycle control protein cdc37 [15].

Other interactions of CDC37

  • Lesions in cdc28 or cdc37 did not suppress any of the ste mutations [16].
  • Suppression is allele specific, and synthetic lethal interactions occur between mps1 and cdc37 alleles [5].
  • The coding regions corresponding to CDC36, CDC37, and CDC39 were then identified and localized by R-loop analysis [7].
  • These data suggest that Cdc37 and Sti1 have functional overlap in stabilizing Hsp90:client complexes [12].
  • We report here the identification of CDC37, which encodes a putative Hsp90 co-chaperone, as a multicopy suppressor of a temperature-sensitive allele (cka2-13(ts)) of the CKA2 gene encoding the alpha' catalytic subunit of protein kinase CKII [17].

Analytical, diagnostic and therapeutic context of CDC37


  1. Induction of human Cdc37 in prostate cancer correlates with the ability of targeted Cdc37 expression to promote prostatic hyperplasia. Stepanova, L., Yang, G., DeMayo, F., Wheeler, T.M., Finegold, M., Thompson, T.C., Harper, J.W. Oncogene (2000) [Pubmed]
  2. Proteome analysis and morphological studies reveal multiple effects of the immunosuppressive drug mycophenolic acid specifically resulting from guanylic nucleotide depletion. Escobar-Henriques, M., Balguerie, A., Monribot, C., Boucherie, H., Daignan-Fornier, B. J. Biol. Chem. (2001) [Pubmed]
  3. Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation. Mandal, A.K., Lee, P., Chen, J.A., Nillegoda, N., Heller, A., Distasio, S., Oen, H., Victor, J., Nair, D.M., Brodsky, J.L., Caplan, A.J. J. Cell Biol. (2007) [Pubmed]
  4. The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability. Lee, P., Rao, J., Fliss, A., Yang, E., Garrett, S., Caplan, A.J. J. Cell Biol. (2002) [Pubmed]
  5. The yeast CDC37 gene interacts with MPS1 and is required for proper execution of spindle pole body duplication. Schutz, A.R., Giddings, T.H., Steiner, E., Winey, M. J. Cell Biol. (1997) [Pubmed]
  6. The KIN28 gene is required both for RNA polymerase II mediated transcription and phosphorylation of the Rpb1p CTD. Valay, J.G., Simon, M., Dubois, M.F., Bensaude, O., Facca, C., Faye, G. J. Mol. Biol. (1995) [Pubmed]
  7. Isolation and transcriptional characterization of three genes which function at start, the controlling event of the Saccharomyces cerevisiae cell division cycle: CDC36, CDC37, and CDC39. Breter, H.J., Ferguson, J., Peterson, T.A., Reed, S.I. Mol. Cell. Biol. (1983) [Pubmed]
  8. Differential in vivo regulation of steroid hormone receptor activation by Cdc37p. Fliss, A.E., Fang, Y., Boschelli, F., Caplan, A.J. Mol. Biol. Cell (1997) [Pubmed]
  9. The oncoprotein kinase chaperone CDC37 functions as an oncogene in mice and collaborates with both c-myc and cyclin D1 in transformation of multiple tissues. Stepanova, L., Finegold, M., DeMayo, F., Schmidt, E.V., Harper, J.W. Mol. Cell. Biol. (2000) [Pubmed]
  10. Genetic interactions among ZDS1,2, CDC37, and protein kinase CK2 in Saccharomyces cerevisiae. Bandhakavi, S., McCann, R.O., Hanna, D.E., Glover, C.V. FEBS Lett. (2003) [Pubmed]
  11. Supervision of multiple signaling protein kinases by the CK2-Cdc37 couple, a possible novel cancer therapeutic target. Miyata, Y., Nishida, E. Ann. N. Y. Acad. Sci. (2004) [Pubmed]
  12. Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase. Lee, P., Shabbir, A., Cardozo, C., Caplan, A.J. Mol. Biol. Cell (2004) [Pubmed]
  13. Physical interaction of Cdc28 with Cdc37 in Saccharomyces cerevisiae. Mort-Bontemps-Soret, M., Facca, C., Faye, G. Mol. Genet. Genomics (2002) [Pubmed]
  14. Cdc37 promotes the stability of protein kinases Cdc28 and Cak1. Farrell, A., Morgan, D.O. Mol. Cell. Biol. (2000) [Pubmed]
  15. The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Pratt, W.B. Proc. Soc. Exp. Biol. Med. (1998) [Pubmed]
  16. Mating-defective ste mutations are suppressed by cell division cycle start mutations in Saccharomyces cerevisiae. Shuster, J.R. Mol. Cell. Biol. (1982) [Pubmed]
  17. A positive feedback loop between protein kinase CKII and Cdc37 promotes the activity of multiple protein kinases. Bandhakavi, S., McCann, R.O., Hanna, D.E., Glover, C.V. J. Biol. Chem. (2003) [Pubmed]
  18. Molecular cloning and cell cycle-dependent expression of a novel gene that is homologous to cdc37. Ozaki, T., Irie, K., Sakiyama, S. DNA Cell Biol. (1995) [Pubmed]
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