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Gene Review

Cdc42  -  CG12530 gene product from transcript...

Drosophila melanogaster

Synonyms: CDC42, CG12530, Cdc42 homolog, Cdc42Dm, D-CDC42, ...
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High impact information on Cdc42

  • Normal patterns of R cell connectivity require Pak's kinase activity and binding sites for both Dock and Cdc42/Rac [1].
  • In line with these observations, a kette phenocopy can be obtained following directed expression of mutant DCDC42 or DRAC1 in the CNS midline [2].
  • Dendrite development is altered in prospero mutants and in transgenic embryos expressing a constitutively active form of the small GTPase cdc42 [3].
  • Dorsal closure can also be blocked by dominant negative Drosophila cdc42, which has been shown to act upstream of JNKK in vertebrates [4].
  • Expressions of analogous mutant Dcdc42 proteins cause qualitatively distinct morphological defects, suggesting that similar GTPases in the same subfamily have unique roles in morphogenesis [5].

Biological context of Cdc42


Anatomical context of Cdc42

  • Besides regulation of kinase activity, another important function of Cdc42 is to recruit Mbt to adherens junctions [6].
  • We found that RhoA and Rac1 have distinct roles in peripheral glial cell migration and nerve ensheathement; however, Cdc42 does not have a significant role in peripheral glial development [9].
  • Cdc42 appears not to be required within macrophages but in other tissues of the embryo to guide macrophages to the ventral trunk region [10].
  • Microinjection of constitutively active Cdc42 (V12Cdc42) disrupts the actomyosin cytoskeleton during cellularization (Crawford et al., Dev. Biol., 204, 151-164 (1998)) [11].
  • A hair begins as a single membrane outgrowth from each wing epithelial cell, and its distal orientation is determined by the restriction of outgrowth to a single distal site on the cell circumference (Wong, L., and P. Adler. 1993. J. Cell Biol. 123:209-211.). We have examined the roles of Cdc42 and Rac1 in the formation of wing hairs [12].

Associations of Cdc42 with chemical compounds

  • We have characterized Drosophila melanogaster ACK (DACK), one of two members of the ACK family of nonreceptor tyrosine kinases in DROSOPHILA: The ACKs are likely effectors for the small GTPase Cdc42, but signaling by these proteins remains poorly defined [13].
  • Of the 10 agents microinjected, C3 exoenzyme, constitutively active Cdc42, and dominant negative Rho have a specific and indistinguishable effect: the actomyosin cytoskeleton is disrupted, cellularization halts, and embryogenesis arrests [14].
  • Down regulation of the leading edge cytoskeleton may be controlled by the serine/threonine kinase DPAK, a potential Drac1/Dcdc42 effector [15].
  • In contrast, we find that association with the key signaling molecules CDC42 and PIP2 is not an essential requirement, implying that activation of Wsp function in vivo depends on additional or alternative signaling pathways [16].

Physical interactions of Cdc42

  • Similarly, in yeast, RotundRacGAP interacts specifically with Drac1 and Dcdc42, as well as with their activated V12 forms, showing a particularly strong interaction with Dcdc42V12 [17].

Regulatory relationships of Cdc42

  • Apical localization of Par-6 requires its interaction with activated Cdc42 and dominant-active or dominant-negative Cdc42 disrupt epithelial polarity, suggesting that activation of this GTPase is crucial for the establishment of epithelial polarity [18].
  • We conclude that Cdc42 regulates aPKC localization and activity downstream of Bazooka, thereby directing neuroblast cell polarity and asymmetric cell division [19].

Other interactions of Cdc42

  • Cdc42 and Rac1 are members of the rho family of small guanosinetriphosphatases and are required for a diverse set of cytoskeleton-membrane interactions in different cell types [20].
  • Drosophila RhoGAP68F is similar to the mammalian protein p50RhoGAP/Cdc42GAP, which exhibits strong GAP activity toward Cdc42 [21].
  • Mbt, a Drosophila PAK protein, combines with Cdc42 to regulate photoreceptor cell morphogenesis [6].
  • In addition, p21-binding domain pull-down assays demonstrate that DRhoGEF4 activates RhoA, but neither Rac1 nor Cdc42 in HEK293 cells [22].
  • Cdc42 binds to a CRIB domain adjacent to the PDZ domain, increasing the affinity of the Par-6 PDZ for its carboxy-terminal ligand by approximately 13-fold [23].


  1. Pak functions downstream of Dock to regulate photoreceptor axon guidance in Drosophila. Hing, H., Xiao, J., Harden, N., Lim, L., Zipursky, S.L. Cell (1999) [Pubmed]
  2. The Drosophila HEM-2/NAP1 homolog KETTE controls axonal pathfinding and cytoskeletal organization. Hummel, T., Leifker, K., Klämbt, C. Genes Dev. (2000) [Pubmed]
  3. Genes regulating dendritic outgrowth, branching, and routing in Drosophila. Gao, F.B., Brenman, J.E., Jan, L.Y., Jan, Y.N. Genes Dev. (1999) [Pubmed]
  4. The Drosophila Jun-N-terminal kinase is required for cell morphogenesis but not for DJun-dependent cell fate specification in the eye. Riesgo-Escovar, J.R., Jenni, M., Fritz, A., Hafen, E. Genes Dev. (1996) [Pubmed]
  5. Distinct morphogenetic functions of similar small GTPases: Drosophila Drac1 is involved in axonal outgrowth and myoblast fusion. Luo, L., Liao, Y.J., Jan, L.Y., Jan, Y.N. Genes Dev. (1994) [Pubmed]
  6. Mbt, a Drosophila PAK protein, combines with Cdc42 to regulate photoreceptor cell morphogenesis. Schneeberger, D., Raabe, T. Development (2003) [Pubmed]
  7. Novel guanine nucleotide exchange factor GEFmeso of Drosophila melanogaster interacts with Ral and Rho GTPase Cdc42. Blanke, S., Jäckle, H. FASEB J. (2006) [Pubmed]
  8. Functional analysis of Cdc42 in actin filament assembly, epithelial morphogenesis, and cell signaling during Drosophila development. Genova, J.L., Jong, S., Camp, J.T., Fehon, R.G. Dev. Biol. (2000) [Pubmed]
  9. RhoA and Rac1 GTPases mediate the dynamic rearrangement of actin in peripheral glia. Sepp, K.J., Auld, V.J. Development (2003) [Pubmed]
  10. Function of Rho GTPases in embryonic blood cell migration in Drosophila. Paladi, M., Tepass, U. J. Cell. Sci. (2004) [Pubmed]
  11. Role of myosin-II phosphorylation in V12Cdc42-mediated disruption of Drosophila cellularization. Crawford, J.M., Su, Z., Varlamova, O., Bresnick, A.R., Kiehart, D.P. Eur. J. Cell Biol. (2001) [Pubmed]
  12. Roles for Rac1 and Cdc42 in planar polarization and hair outgrowth in the wing of Drosophila. Eaton, S., Wepf, R., Simons, K. J. Cell Biol. (1996) [Pubmed]
  13. ACK family tyrosine kinase activity is a component of Dcdc42 signaling during dorsal closure in Drosophila melanogaster. Sem, K.P., Zahedi, B., Tan, I., Deak, M., Lim, L., Harden, N. Mol. Cell. Biol. (2002) [Pubmed]
  14. Cellularization in Drosophila melanogaster is disrupted by the inhibition of rho activity and the activation of Cdc42 function. Crawford, J.M., Harden, N., Leung, T., Lim, L., Kiehart, D.P. Dev. Biol. (1998) [Pubmed]
  15. Participation of small GTPases in dorsal closure of the Drosophila embryo: distinct roles for Rho subfamily proteins in epithelial morphogenesis. Harden, N., Ricos, M., Ong, Y.M., Chia, W., Lim, L. J. Cell. Sci. (1999) [Pubmed]
  16. Conserved interactions with cytoskeletal but not signaling elements are an essential aspect of Drosophila WASp function. Tal, T., Vaizel-Ohayon, D., Schejter, E.D. Dev. Biol. (2002) [Pubmed]
  17. The Rac GTPase-activating protein RotundRacGAP interferes with Drac1 and Dcdc42 signalling in Drosophila melanogaster. Raymond, K., Bergeret, E., Dagher, M.C., Breton, R., Griffin-Shea, R., Fauvarque, M.O. J. Biol. Chem. (2001) [Pubmed]
  18. Sequential roles of Cdc42, Par-6, aPKC, and Lgl in the establishment of epithelial polarity during Drosophila embryogenesis. Hutterer, A., Betschinger, J., Petronczki, M., Knoblich, J.A. Dev. Cell (2004) [Pubmed]
  19. Cdc42 acts downstream of Bazooka to regulate neuroblast polarity through Par-6 aPKC. Atwood, S.X., Chabu, C., Penkert, R.R., Doe, C.Q., Prehoda, K.E. J. Cell. Sci. (2007) [Pubmed]
  20. CDC42 and Rac1 control different actin-dependent processes in the Drosophila wing disc epithelium. Eaton, S., Auvinen, P., Luo, L., Jan, Y.N., Simons, K. J. Cell Biol. (1995) [Pubmed]
  21. Drosophila RhoGAP68F is a putative GTPase activating protein for RhoA participating in gastrulation. Sanny, J., Chui, V., Langmann, C., Pereira, C., Zahedi, B., Harden, N. Dev. Genes Evol. (2006) [Pubmed]
  22. Drosophila RhoGEF4 encodes a novel RhoA-specific guanine exchange factor that is highly expressed in the embryonic central nervous system. Nahm, M., Lee, M., Baek, S.H., Yoon, J.H., Kim, H.H., Lee, Z.H., Lee, S. Gene (2006) [Pubmed]
  23. Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition. Peterson, F.C., Penkert, R.R., Volkman, B.F., Prehoda, K.E. Mol. Cell (2004) [Pubmed]
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