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Gene Review

CDC25  -  Cdc25p

Saccharomyces cerevisiae S288c

Synonyms: CTN1, Cell division control protein 25, L2142.6, YLR310C
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Disease relevance of CDC25

  • When expressed in E. coli, the chimeric product is detectable by antibodies directed against the carboxy-terminal CDC25 peptide and has an exchange-factor activity on the Ras2 protein [1].
  • Recently, significant sequence homologies were found with an antigen from Onchocerca volvulus, a fruit fly odorant-binding protein and the yeast protein TFS1 which is a dosage-dependent suppressor of CDC25 mutations [2].

High impact information on CDC25

  • The BUD5 nucleotide sequence predicts a protein of 538 amino acids that has similarity to the S. cerevisiae CDC25 product, an activator of RAS proteins that catalyzes GDP-GTP exchange [3].
  • Functional cloning of BUD5, a CDC25-related gene from S. cerevisiae that can suppress a dominant-negative RAS2 mutant [4].
  • Furthermore, these dominant Ha-ras mutations have the appropriate phenotype in mammalian cells, suggesting the presence of a CDC25-like protein [5].
  • For example, the human H-ras gene can substitute for yeast RAS; the relationship is sufficiently close that dominant Ha-ras mutations that inhibit CDC25 have been found (Powers et al., 1989) [5].
  • They also have found a meiotic level of message in temperature-sensitive cdc25 diploids shifted to high temperature in rich medium (Simchen and Kassir, 1989) [5].

Biological context of CDC25

  • Furthermore, mutationally activated alleles of CDC25 are capable of inducing a set of phenotypes similar to those observed in strains containing a genetically activated RAS/adenylate cyclase pathway, suggesting that CDC25 encodes a regulatory protein [6].
  • The lethality resulting from disruption of the CDC25 gene can be suppressed by the presence of the activated RAS2val19 gene, but not by high copy plasmids expressing a normal RAS2 or RAS1 gene [6].
  • The evidence presented here indicates that CDC25, identified by conditional cell cycle arrest mutations, encodes such an upstream function [7].
  • The rate of enzyme activation in the presence of non-hydrolysable analogs of GTP increases with the number of CDC25 gene copies present in the cell [8].
  • These results support a model in which the CDC25 gene product is the GDP-GTP exchange factor regulating the activity of the RAS gene product [9].

Anatomical context of CDC25

  • The attenuated GTP regulation adenylyl cyclase (CDC35) lysates or membranes prepared from cells of a cdc25ts strain is enhanced 2.5- to 6-fold by mixing these lysates or membranes with lysates or membranes from a cdc35ts strain harboring wild-type CDC25 [8].
  • These data suggest that Cdc25 might not be required in certain conditions for the guanine nucleotide exchange reaction in Ras and that it might be implicated in anchoring the Ras/adenylate cyclase system to the plasma membrane [10].
  • Homologues of ste6 and CDC25 could regulate ras activity in other eukaryotic cells [11].
  • The evidence presented here indicates that the domain containing the COOH-terminal part of the Saccharomyces cerevisiae SCD25 gene product (C-domain), which is homologous to the COOH-terminal part of CDC25 protein, can elicit activation of mammalian ras proteins in CHO cells [12].
  • The arrest of the cell cycle appears to be independent of the carbon and nitrogen sources, and the cell wall of cdc25-arrested cells shows changes similar to those found in cells undergoing entry in to the stationary phase [13].

Associations of CDC25 with chemical compounds


Physical interactions of CDC25


Regulatory relationships of CDC25

  • Anti-Cdc25 antibodies inhibit guanyl nucleotide-dependent adenylyl cyclase of Saccharomyces cerevisiae and cross-react with a 150-kilodalton mammalian protein [19].
  • In contrast with the C-terminal part, the complete SDC25 gene was found not to suppress the CDC25 gene defect [20].
  • The ability of TFS1 to suppress cdc25 is allele specific: the temperature-sensitive cdc25-1 mutation is suppressed efficiently but the cdc25-5 mutation and two disruption mutations are only partially suppressed [21].
  • These results suggest that the Cdc25 factor might also control Gpa2p [22].
  • Our results support a Cdc14 conserved inhibitory mechanism acting on S. pombe Cdc25 protein and suggest that human cells may regulate Cdc25 in a similar manner to inactivate Cdk1-mitotic cyclin complexes [23].

Other interactions of CDC25

  • We have previously demonstrated that the IRA1-encoded protein inhibits the function of the RAS protein in a fashion antagonistic to the function of the CDC25 protein in the RAS-cAMP pathway in Saccharomyces cerevisiae [24].
  • In the yeast Saccharomyces cerevisiae, the activation of adenylate cyclase requires the products of the RAS genes and of CDC25 [9].
  • Genetic data suggest that the yeast cell cycle control gene CDC25 is an upstream regulator of RAS2 [15].
  • LTE1 belongs to the CDC25 family that encodes a guanine nucleotide exchange factor for GTP-binding proteins of the ras family [25].
  • CDC3, CDC25 and CDC42 were localized to chromosome XII by hybridizing the cloned genes to Southern blots of chromosomes separated by orthogonal-field-alternation gel electrophoresis [26].

Analytical, diagnostic and therapeutic context of CDC25


  1. The C-terminal part of the CDC25 gene product has Ras-nucleotide exchange activity when present in a chimeric SDC25-CDC25 protein. Boy-Marcotte, E., Buu, A., Soustelle, C., Poullet, P., Parmeggiani, A., Jacquet, M. Curr. Genet. (1993) [Pubmed]
  2. From structure to function: possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site. Schoentgen, F., Jollès, P. FEBS Lett. (1995) [Pubmed]
  3. Yeast BUD5, encoding a putative GDP-GTP exchange factor, is necessary for bud site selection and interacts with bud formation gene BEM1. Chant, J., Corrado, K., Pringle, J.R., Herskowitz, I. Cell (1991) [Pubmed]
  4. Functional cloning of BUD5, a CDC25-related gene from S. cerevisiae that can suppress a dominant-negative RAS2 mutant. Powers, S., Gonzales, E., Christensen, T., Cubert, J., Broek, D. Cell (1991) [Pubmed]
  5. Dual regulation of meiosis in yeast. Malone, R.E. Cell (1990) [Pubmed]
  6. The S. cerevisiae CDC25 gene product regulates the RAS/adenylate cyclase pathway. Broek, D., Toda, T., Michaeli, T., Levin, L., Birchmeier, C., Zoller, M., Powers, S., Wigler, M. Cell (1987) [Pubmed]
  7. CDC25: a component of the RAS-adenylate cyclase pathway in Saccharomyces cerevisiae. Robinson, L.C., Gibbs, J.B., Marshall, M.S., Sigal, I.S., Tatchell, K. Science (1987) [Pubmed]
  8. In vitro reconstitution of cdc25 regulated S. cerevisiae adenylyl cyclase and its kinetic properties. Engelberg, D., Simchen, G., Levitzki, A. EMBO J. (1990) [Pubmed]
  9. A new RAS mutation that suppresses the CDC25 gene requirement for growth of Saccharomyces cerevisiae. Camonis, J.H., Jacquet, M. Mol. Cell. Biol. (1988) [Pubmed]
  10. Activation of adenylate cyclase in cdc25 mutants of Saccharomyces cerevisiae. Pardo, L.A., Lazo, P.S., Ramos, S. FEBS Lett. (1993) [Pubmed]
  11. Homologous activators of ras in fission and budding yeast. Hughes, D.A., Fukui, Y., Yamamoto, M. Nature (1990) [Pubmed]
  12. The COOH-domain of the product of the Saccharomyces cerevisiae SCD25 gene elicits activation of p21-ras proteins in mammalian cells. Rey, I., Schweighoffer, F., Barlat, I., Camonis, J., Boy-Marcotte, E., Guilbaud, R., Jacquet, M., Tocque, B. Oncogene (1991) [Pubmed]
  13. Macromolecular syntheses in the cell cycle mutant cdc25 of budding yeast. Martegani, E., Vanoni, M., Baroni, M. Eur. J. Biochem. (1984) [Pubmed]
  14. SDC25, a dispensable Ras guanine nucleotide exchange factor of Saccharomyces cerevisiae differs from CDC25 by its regulation. Boy-Marcotte, E., Ikonomi, P., Jacquet, M. Mol. Biol. Cell (1996) [Pubmed]
  15. The Saccharomyces cerevisiae CDC25 gene product binds specifically to catalytically inactive ras proteins in vivo. Munder, T., Fürst, P. Mol. Cell. Biol. (1992) [Pubmed]
  16. The SH3 domain of the S. cerevisiae Cdc25p binds adenylyl cyclase and facilitates Ras regulation of cAMP signalling. Mintzer, K.A., Field, J. Cell. Signal. (1999) [Pubmed]
  17. Ssa1p chaperone interacts with the guanine nucleotide exchange factor of ras Cdc25p and controls the cAMP pathway in Saccharomyces cerevisiae. Geymonat, M., Wang, L., Garreau, H., Jacquet, M. Mol. Microbiol. (1998) [Pubmed]
  18. The glyceraldehyde-3-phosphate dehydrogenase binds in vitro to the SH3 domain of Saccharomyces cerevisiae Cdc25p. Buu, A., Garreau, H., Jacquet, M. C. R. Acad. Sci. III, Sci. Vie (1995) [Pubmed]
  19. Anti-Cdc25 antibodies inhibit guanyl nucleotide-dependent adenylyl cyclase of Saccharomyces cerevisiae and cross-react with a 150-kilodalton mammalian protein. Gross, E., Marbach, I., Engelberg, D., Segal, M., Simchen, G., Levitzki, A. Mol. Cell. Biol. (1992) [Pubmed]
  20. SDC25, a CDC25-like gene which contains a RAS-activating domain and is a dispensable gene of Saccharomyces cerevisiae. Damak, F., Boy-Marcotte, E., Le-Roscouet, D., Guilbaud, R., Jacquet, M. Mol. Cell. Biol. (1991) [Pubmed]
  21. TFS1: a suppressor of cdc25 mutations in Saccharomyces cerevisiae. Robinson, L.C., Tatchell, K. Mol. Gen. Genet. (1991) [Pubmed]
  22. At acidic pH, the diminished hypoxic expression of the SRP1/TIR1 yeast gene depends on the GPA2-cAMP and HOG pathways. Bourdineaud, J.P. Res. Microbiol. (2000) [Pubmed]
  23. Functional homology among human and fission yeast Cdc14 phosphatases. Vázquez-Novelle, M.D., Esteban, V., Bueno, A., Sacristán, M.P. J. Biol. Chem. (2005) [Pubmed]
  24. MSI1, a negative regulator of the RAS-cAMP pathway in Saccharomyces cerevisiae. Ruggieri, R., Tanaka, K., Nakafuku, M., Kaziro, Y., Toh-e, A., Matsumoto, K. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  25. The yeast TEM1 gene, which encodes a GTP-binding protein, is involved in termination of M phase. Shirayama, M., Matsui, Y., Toh-E, A. Mol. Cell. Biol. (1994) [Pubmed]
  26. Mapping of the Saccharomyces cerevisiae CDC3, CDC25, and CDC42 genes to chromosome XII by chromosome blotting and tetrad analysis. Johnson, D.I., Jacobs, C.W., Pringle, J.R., Robinson, L.C., Carle, G.F., Olson, M.V. Yeast (1987) [Pubmed]
  27. Mutagenic alteration of the distal switch II region of RAS blocks CDC25-dependent signaling functions. Mirisola, M.G., Seidita, G., Verrotti, A.C., Di Blasi, F., Fasano, O. J. Biol. Chem. (1994) [Pubmed]
  28. Characterization, cloning and sequence analysis of the CDC25 gene which controls the cyclic AMP level of Saccharomyces cerevisiae. Camonis, J.H., Kalékine, M., Gondré, B., Garreau, H., Boy-Marcotte, E., Jacquet, M. EMBO J. (1986) [Pubmed]
  29. Site-directed mutagenesis of the Saccharomyces cerevisiae CDC25 gene: effects on mitotic growth and cAMP signalling. Schomerus, C., Munder, T., Küntzel, H. Mol. Gen. Genet. (1990) [Pubmed]
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