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Gene Review

CDC42  -  Rho family GTPase CDC42

Saccharomyces cerevisiae S288c

Synonyms: Cell division control protein 42, L8083.13, SRO2, Suppressor of RHO3 protein 2, YLR229C
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Disease relevance of CDC42

  • Moreover, we report that Salmonella SptP can act as a GAP for Cdc42 in S. cerevisiae, down-regulating MAPK-mediated signaling [1].
  • Isolation of mutations in the Drosophila homologues of the human Neurofibromatosis 2 and yeast CDC42 genes using a simple and efficient reverse-genetic method [2].
  • Interestingly, expression of membrane-targeted Far1p causes toxicity, most likely by activating Cdc42p uniformly at the cell cortex [3].

Psychiatry related information on CDC42

  • Analysis using this assay further demonstrated that the motor activity of these myosins is required for the polymerization step, and that actin polymerization depends on phosphorylation of myosin motor domain by p21-activated kinases (PAKs), downstream effectors of the small guanosine triphosphatase, Cdc42p [4].

High impact information on CDC42

  • In the organization of the bud site or of the site in which a mating projection appears, Cdc42, its activator Cdc24, and its negative regulators play a fundamental role [5].
  • In the absence of Cdc42 or Cdc24, the actin cytoskeleton does not become organized and budding does not take place [5].
  • The Ras-related GTP-binding protein Cdc42 is implicated in a variety of biological activities including the establishment of cell polarity in yeast, the regulation of cell morphology, motility and cell-cycle progression in mammalian cells and the induction of malignant transformation [6].
  • We identified a Cdc42 mutant (Cdc42F28L) which binds GTP in the absence of a guanine nucleotide exchange factor, but still hydrolyses GTP with a turnover number identical to that for wild-type Cdc42 [6].
  • The polarization of yeast cells shares many features with that of these more complex examples, including regulation by both intrinsic and extrinsic cues, conserved regulatory molecules such as Cdc42 GTPase, and asymmetry of the cytoskeleton as its centerpiece [7].

Biological context of CDC42


Anatomical context of CDC42

  • In some strains, the ability of CDC42 to serve as a multicopy suppressor of the Ts- growth defect of deltabem4 cells required co-overexpression of Rho1p, which is an essential Rho-type GTPase necessary for cell wall integrity [13].
  • For CDC42 controlled bud assembly in yeast, the components of the plasma-membrane complex are not so clear [14].
  • Incorporation of the available data on rac in neutrophils, CDC42 in yeast, and rho in fibroblasts suggests a general model for the function of rho-like GTPase (Figure 1) [14].
  • The AgCDC42 and AgCDC24 genes can both complement conditional mutations in the S. cerevisiae CDC42 and CDC24 genes and both proteins are required for the establishment of actin polarization in A. gossypii germ cells [15].
  • Bni1p may function as a Cdc42p target that links the pheromone response pathway to the actin cytoskeleton [11].

Associations of CDC42 with chemical compounds

  • Actin incorporation in the bud can be stimulated by treating the permeabilized cells with GTP-gamma S, and, significantly, the stimulatory effect is eliminated by a mutation in CDC42, a gene that encodes a Rho-like GTP-binding protein required for bud formation [16].
  • Ste20/PAK serine/threonine protein kinases have been suggested as playing essential roles in cell signalling and morphogenesis as potential targets of Cdc42 and Rac GTPases [17].
  • Cdc24p is the guanine-nucleotide exchange factor for the Cdc42p GTPase, which controls cell polarity in Saccharomyces cerevisiae [18].
  • We have analyzed the effects of three CDC42 mutations (Gly to Val-12, Gln to Leu-61, and Asp to Ala-118) in the putative GTP-binding and hydrolysis domains and one mutation (Cys to Ser-188) in the putative isoprenylation site [19].
  • The Pak1 protein autophosphorylates on serine residues and preferentially binds to activated Cdc42p both in vitro and in vivo [20].

Physical interactions of CDC42


Regulatory relationships of CDC42

  • These results suggest that Cdc42 is closely involved in regulating actin assembly during polarized cell growth [16].
  • However, one of the other genes that was isolated by virtue of its ability to suppress cdc24 can also suppress cdc42 [25].
  • Cla4p kinase was activated in vivo by the GTP-bound form of Cdc42p [26].
  • Elevated levels of STE20 and BEM1 are capable of suppressing a temperature-sensitive mutation in CDC42 [27].
  • RA domain function can be replaced by the nine C-terminal, plasma membrane-targeting residues (KKSKKCAIL) of Cdc42, and membrane-targeted Ste50 also suppresses the signaling deficiency of cdc42 alleles specifically defective in invasive growth [28].
  • We show that Bem1p promotes symmetry breaking by assembling a complex in which both a Cdc42p-directed guanine nucleotide exchange factor (GEF) and a Cdc42p effector p21-activated kinase (PAK) associate with Bem1p [29].

Other interactions of CDC42

  • Therefore, the inability of cdc24 and cdc42 mutants to mate has been presumed to be due to a requirement for generation of cell polarity and related morphogenetic events during conjugation [8].
  • Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway [30].
  • CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae [31].
  • One of these proved to be CDC42, which has previously been shown to be a member of the rho (ras-homologous) family of genes, and a second is a newly identified ras-related gene that we named RSR1 [25].
  • Ste20, which phosphorylates Ste11 to initiate signaling, is activated by binding to Cdc42 GTPase (membrane anchored via its C-terminal geranylgeranylation) [28].

Analytical, diagnostic and therapeutic context of CDC42

  • Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42 [32].
  • Each protein contains a CRIB (Cdc42/Rac-interactive binding) motif and each interacts in the two-hybrid assay with the GTP-bound form of the Rho-type Cdc42 GTPase, a key regulator of polarized growth in yeast [33].
  • Association of RhoA and CDC42 with RhoGDI was further suggested by coelution of these proteins with RhoGDI at an estimated size of approximately 45 kDa after gel-filtration chromatography [34].
  • Gel overlay assays and affinity chromatography experiments showed that MIHCK interacted with GTPgammaS (guanosine 5'-3-O-(thiotriphosphate))-labeled Cdc42 and Rac1 but not RhoA [35].
  • Using cell fractionation and immunolocalization techniques, we have investigated the subcellular localization of Cdc42p [36].


  1. A novel connection between the yeast Cdc42 GTPase and the Slt2-mediated cell integrity pathway identified through the effect of secreted Salmonella GTPase modulators. Rodríguez-Pachón, J.M., Martín, H., North, G., Rotger, R., Nombela, C., Molina, M. J. Biol. Chem. (2002) [Pubmed]
  2. Isolation of mutations in the Drosophila homologues of the human Neurofibromatosis 2 and yeast CDC42 genes using a simple and efficient reverse-genetic method. Fehon, R.G., Oren, T., LaJeunesse, D.R., Melby, T.E., McCartney, B.M. Genetics (1997) [Pubmed]
  3. Site-specific regulation of the GEF Cdc24p by the scaffold protein Far1p during yeast mating. Wiget, P., Shimada, Y., Butty, A.C., Bi, E., Peter, M. EMBO J. (2004) [Pubmed]
  4. Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization. Lechler, T., Shevchenko, A., Li, R. J. Cell Biol. (2000) [Pubmed]
  5. Role of small G proteins in yeast cell polarization and wall biosynthesis. Cabib, E., Drgonová, J., Drgon, T. Annu. Rev. Biochem. (1998) [Pubmed]
  6. The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation. Wu, W.J., Erickson, J.W., Lin, R., Cerione, R.A. Nature (2000) [Pubmed]
  7. Cell polarity in yeast. Chant, J. Annu. Rev. Cell Dev. Biol. (1999) [Pubmed]
  8. Role for the Rho-family GTPase Cdc42 in yeast mating-pheromone signal pathway. Simon, M.N., De Virgilio, C., Souza, B., Pringle, J.R., Abo, A., Reed, S.I. Nature (1995) [Pubmed]
  9. Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small GTP binding protein in Saccharomyces cerevisiae. Ozaki, K., Tanaka, K., Imamura, H., Hihara, T., Kameyama, T., Nonaka, H., Hirano, H., Matsuura, Y., Takai, Y. EMBO J. (1996) [Pubmed]
  10. TFS1: a suppressor of cdc25 mutations in Saccharomyces cerevisiae. Robinson, L.C., Tatchell, K. Mol. Gen. Genet. (1991) [Pubmed]
  11. Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Evangelista, M., Blundell, K., Longtine, M.S., Chow, C.J., Adames, N., Pringle, J.R., Peter, M., Boone, C. Science (1997) [Pubmed]
  12. Novel Cdc42-binding proteins Gic1 and Gic2 control cell polarity in yeast. Brown, J.L., Jaquenoud, M., Gulli, M.P., Chant, J., Peter, M. Genes Dev. (1997) [Pubmed]
  13. Identification of the bud emergence gene BEM4 and its interactions with rho-type GTPases in Saccharomyces cerevisiae. Mack, D., Nishimura, K., Dennehey, B.K., Arbogast, T., Parkinson, J., Toh-e, A., Pringle, J.R., Bender, A., Matsui, Y. Mol. Cell. Biol. (1996) [Pubmed]
  14. Ras-related GTPases and the cytoskeleton. Hall, A. Mol. Biol. Cell (1992) [Pubmed]
  15. Cell polarity and hyphal morphogenesis are controlled by multiple rho-protein modules in the filamentous ascomycete Ashbya gossypii. Wendland, J., Philippsen, P. Genetics (2001) [Pubmed]
  16. Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast. Li, R., Zheng, Y., Drubin, D.G. J. Cell Biol. (1995) [Pubmed]
  17. Characterization of SKM1, a Saccharomyces cerevisiae gene encoding a novel Ste20/PAK-like protein kinase. Martín, H., Mendoza, A., Rodríguez-Pachón, J.M., Molina, M., Nombela, C. Mol. Microbiol. (1997) [Pubmed]
  18. Characterization of synthetic-lethal mutants reveals a role for the Saccharomyces cerevisiae guanine-nucleotide exchange factor Cdc24p in vacuole function and Na+ tolerance. White, W.H., Johnson, D.I. Genetics (1997) [Pubmed]
  19. Mutational analysis of CDC42Sc, a Saccharomyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity. Ziman, M., O'Brien, J.M., Ouellette, L.A., Church, W.R., Johnson, D.I. Mol. Cell. Biol. (1991) [Pubmed]
  20. Fission yeast pak1+ encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating. Ottilie, S., Miller, P.J., Johnson, D.I., Creasy, C.L., Sells, M.A., Bagrodia, S., Forsburg, S.L., Chernoff, J. EMBO J. (1995) [Pubmed]
  21. Interaction between a Ras and a Rho GTPase couples selection of a growth site to the development of cell polarity in yeast. Kozminski, K.G., Beven, L., Angerman, E., Tong, A.H., Boone, C., Park, H.O. Mol. Biol. Cell (2003) [Pubmed]
  22. Iqg1p, a yeast homologue of the mammalian IQGAPs, mediates cdc42p effects on the actin cytoskeleton. Osman, M.A., Cerione, R.A. J. Cell Biol. (1998) [Pubmed]
  23. Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast. Cvrcková, F., De Virgilio, C., Manser, E., Pringle, J.R., Nasmyth, K. Genes Dev. (1995) [Pubmed]
  24. Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAPK pathway. Raitt, D.C., Posas, F., Saito, H. EMBO J. (2000) [Pubmed]
  25. Multicopy suppression of the cdc24 budding defect in yeast by CDC42 and three newly identified genes including the ras-related gene RSR1. Bender, A., Pringle, J.R. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  26. Cla4p, a Saccharomyces cerevisiae Cdc42p-activated kinase involved in cytokinesis, is activated at mitosis. Benton, B.K., Tinkelenberg, A., Gonzalez, I., Cross, F.R. Mol. Cell. Biol. (1997) [Pubmed]
  27. Genetic interactions indicate a role for Mdg1p and the SH3 domain protein Bem1p in linking the G-protein mediated yeast pheromone signalling pathway to regulators of cell polarity. Leberer, E., Chenevert, J., Leeuw, T., Harcus, D., Herskowitz, I., Thomas, D.Y. Mol. Gen. Genet. (1996) [Pubmed]
  28. The RA domain of Ste50 adaptor protein is required for delivery of Ste11 to the plasma membrane in the filamentous growth signaling pathway of the yeast Saccharomyces cerevisiae. Truckses, D.M., Bloomekatz, J.E., Thorner, J. Mol. Cell. Biol. (2006) [Pubmed]
  29. Symmetry-breaking polarization driven by a Cdc42p GEF-PAK complex. Kozubowski, L., Saito, K., Johnson, J.M., Howell, A.S., Zyla, T.R., Lew, D.J. Curr. Biol. (2008) [Pubmed]
  30. Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway. Tatebayashi, K., Yamamoto, K., Tanaka, K., Tomida, T., Maruoka, T., Kasukawa, E., Saito, H. EMBO J. (2006) [Pubmed]
  31. CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae. Adams, A.E., Johnson, D.I., Longnecker, R.M., Sloat, B.F., Pringle, J.R. J. Cell Biol. (1990) [Pubmed]
  32. Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. Shinjo, K., Koland, J.G., Hart, M.J., Narasimhan, V., Johnson, D.I., Evans, T., Cerione, R.A. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  33. The Cdc42 GTPase-associated proteins Gic1 and Gic2 are required for polarized cell growth in Saccharomyces cerevisiae. Chen, G.C., Kim, Y.J., Chan, C.S. Genes Dev. (1997) [Pubmed]
  34. Subcellular distribution and membrane association of Rho-related small GTP-binding proteins in kidney cortex. Boivin, D., Béliveau, R. Am. J. Physiol. (1995) [Pubmed]
  35. Cloning and characterization of a Dictyostelium myosin I heavy chain kinase activated by Cdc42 and Rac. Lee, S.F., Egelhoff, T.T., Mahasneh, A., Côté, G.P. J. Biol. Chem. (1996) [Pubmed]
  36. Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity. Ziman, M., Preuss, D., Mulholland, J., O'Brien, J.M., Botstein, D., Johnson, D.I. Mol. Biol. Cell (1993) [Pubmed]
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