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Gene Review

CDC12  -  septin CDC12

Saccharomyces cerevisiae S288c

Synonyms: CLA10, Cell division control protein 12, PSL7, Septin, YHR107C
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Disease relevance of CDC12


High impact information on CDC12

  • Siz1 is required for SUMO attachment to the S. cerevisiae septins in vivo and strongly stimulates septin sumoylation in vitro [3].
  • Sec3-GFP localization is independent of secretory pathway function, of the actin and septin cytoskeletons, and of the polarity establishment proteins [4].
  • Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier [5].
  • Higher-order septin assemblies represented by the yeast septin collar function as cytoskeleton, providing structural support and scaffolds for many cellular factors [6].
  • Recent studies revealed that septin populations with no obvious structure that had previously escaped our attention serve as scaffolds for kinetochore motor proteins and as sequestering depots for microtubule regulators [6].

Biological context of CDC12

  • Interestingly, a cdc5Delta bfa1Delta swe1Delta triple mutant is viable but grows slowly, whereas cdc5Delta cells bearing both CDC5DeltaC-CNM67 and CDC5DeltaC-CDC12 grow well with only a mild cell cycle delay [7].
  • The second suppressor maps to the right arm of chromosome VIII distal to CDC12 and is REC104, a meiosis-specific gene believed to act early in meiosis [8].
  • Cla4 and Ste20 kinases apparently share a function in localizing cell growth with respect to the septin ring [9].
  • Thus, septin collar formation may correspond to septin filament assembly, and requires both GTP binding and Cla4-mediated phosphorylation of septins [10].
  • In vivo, mutants unable to bind GTP prevent septin collar formation, whereas mutants that block GTP hydrolysis do not [10].

Anatomical context of CDC12

  • Examination of mating cells and cells responding to purified mating pheromone revealed novel arrangements of the CDC3 and CDC12 products in the regions of cell wall reorganization [11].
  • Our results suggest that polarisome components and Cla4p are required for the initial assembly of the septin ring and that the actin cytoskeleton is involved in this process [12].
  • Thus, placement of the Int1p/septin ring with respect to the mother-daughter cell junction distinguishes yeast/pseudohyphal growth from hyphal growth in C. albicans [13].
  • Using a septin-GFP fusion and time-lapse confocal microscopy, we have determined that septin dynamics are maintained in budding zygotes and during unipolar synchronous growth in pseudohyphae [14].
  • Budding cells of the yeast Saccharomyces cerevisiae possess a ring of septin filaments of unknown biochemical nature that lies under the inner surface of the plasma membrane in the neck that connects the mother cell to its bud [15].

Associations of CDC12 with chemical compounds

  • Consistently, treatment of cla4Delta mutant with the actin inhibitor latrunculin A inhibited septin ring assembly [12].
  • The septin polypeptides show various degrees of saturation with guanine nucleotides in different complexes [16].
  • Glutaraldehyde-fixed rat brain sec6/8 complex adopts a conformation resembling the letter "T" or "Y". The sec6/8 and septin complexes likely play an important role in trafficking vesicles and organizing proteins at the plasma membrane of neurons [17].
  • In this pathway, insults affecting the actin or septin cytoskeleton trigger a cell cycle arrest, mediated by the Wee1 homolog Swe1p, which catalyzes the inhibitory phosphorylation of the mitosis-promoting cyclin-dependent kinase (CDK) on a conserved tyrosine residue [18].
  • Both localizations are septin-independent and disrupted by treatment with filipin [19].

Physical interactions of CDC12

  • To investigate the relationship between these filaments and the neck filaments, we purified septin complexes from cells deleted for CDC10 or CDC11 [20].
  • In addition, Cdc11 forms a stoichiometric complex with Cdc12, independent of its CTE [21].
  • Candida albicans Int1p interacts with the septin ring in yeast and hyphal cells [13].
  • Shs1p: a novel member of septin that interacts with spa2p, involved in polarized growth in saccharomyces cerevisiae [22].
  • Afr1p interacts with Cdc12p, which belongs to a family of filament-forming proteins termed septins that have been studied primarily for their role in bud morphogenesis and cytokinesis [23].

Enzymatic interactions of CDC12


Regulatory relationships of CDC12

  • This defect is greatly exacerbated when combined with GTP binding-defective septins; conversely, the septin collar assembly defect of such mutants is suppressed efficiently by CLA4 overexpression [10].
  • Septin recruitment depends on activated Cdc42p but not on the normal pathway for bud-site selection [25].
  • Apical polarization was delayed in cdc15 mutants as compared with budding in control cells and this delay was abolished in a septin mutant [26].
  • Specifically, we show that septin ring separation and disassembly is delayed in anaphase, suggesting that CBF3 regulates septin dynamics [27].
  • In addition to localizing at the spindle poles and cytokinetic neck filaments, Cdc5 induces and localizes to additional septin ring structures within the elongated buds [28].

Other interactions of CDC12

  • However, double cla4 ste20 mutants cannot maintain septin rings at the bud neck and cannot undergo cytokinesis [9].
  • We also used the CDC3-specific and CDC12-specific antibodies to investigate the timing of localization of these proteins to the budding site [11].
  • GTP binding-defective Cdc10 and Cdc12 form soluble heteromeric complexes with other septins both in yeast and in bacteria; yet, unlike wild-type, mutant complexes do not bind GTP and do not assemble into filaments in vitro [10].
  • A search for additional S. cerevisiae septin genes using the polymerase chain reaction identified SPR3, a gene that had been identified previously on the basis of its sporulation-specific expression [29].
  • In contrast, mutations affecting the other two Nim1p-related kinases in S. cerevisiae, Hsl1p and Kcc4p, produce no detectable effect on septin organization [30].

Analytical, diagnostic and therapeutic context of CDC12


  1. Expression of Nedd5, a mammalian septin, in human brain tumors. Sakai, K., Kurimoto, M., Tsugu, A., Hubbard, S.L., Trimble, W.S., Rutka, J.T. J. Neurooncol. (2002) [Pubmed]
  2. An RNA-Binding Protein, hnRNP A1, and a Scaffold Protein, Septin 6, Facilitate Hepatitis C Virus Replication. Kim, C.S., Seol, S.K., Song, O.K., Park, J.H., Jang, S.K. J. Virol. (2007) [Pubmed]
  3. An E3-like factor that promotes SUMO conjugation to the yeast septins. Johnson, E.S., Gupta, A.A. Cell (2001) [Pubmed]
  4. Sec3p is a spatial landmark for polarized secretion in budding yeast. Finger, F.P., Hughes, T.E., Novick, P. Cell (1998) [Pubmed]
  5. Plasma membrane compartmentalization in yeast by messenger RNA transport and a septin diffusion barrier. Takizawa, P.A., DeRisi, J.L., Wilhelm, J.E., Vale, R.D. Science (2000) [Pubmed]
  6. Diversity of septin scaffolds. Kinoshita, M. Curr. Opin. Cell Biol. (2006) [Pubmed]
  7. Novel functional dissection of the localization-specific roles of budding yeast polo kinase Cdc5p. Park, J.E., Park, C.J., Sakchaisri, K., Karpova, T., Asano, S., McNally, J., Sunwoo, Y., Leem, S.H., Lee, K.S. Mol. Cell. Biol. (2004) [Pubmed]
  8. A conditional allele of the Saccharomyces cerevisiae HOP1 gene is suppressed by overexpression of two other meiosis-specific genes: RED1 and REC104. Hollingsworth, N.M., Johnson, A.D. Genetics (1993) [Pubmed]
  9. 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]
  10. Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK, Cla4. Versele, M., Thorner, J. J. Cell Biol. (2004) [Pubmed]
  11. Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC3 gene product and the timing of events at the budding site. Kim, H.B., Haarer, B.K., Pringle, J.R. J. Cell Biol. (1991) [Pubmed]
  12. Septin ring assembly requires concerted action of polarisome components, a PAK kinase Cla4p, and the actin cytoskeleton in Saccharomyces cerevisiae. Kadota, J., Yamamoto, T., Yoshiuchi, S., Bi, E., Tanaka, K. Mol. Biol. Cell (2004) [Pubmed]
  13. Candida albicans Int1p interacts with the septin ring in yeast and hyphal cells. Gale, C., Gerami-Nejad, M., McClellan, M., Vandoninck, S., Longtine, M.S., Berman, J. Mol. Biol. Cell (2001) [Pubmed]
  14. Cell cycle control of septin ring dynamics in the budding yeast. Cid, V.J., Adamiková, L., Sánchez, M., Molina, M., Nombela, C. Microbiology (Reading, Engl.) (2001) [Pubmed]
  15. Characterization of the CDC10 product and the timing of events of the budding site of Saccharomyces cerevisiae. Jeong, J.W., Kim, D.H., Choi, S.Y., Kim, H.B. Mol. Cells (2001) [Pubmed]
  16. Nucleotide binding and filament assembly of recombinant yeast septin complexes. Farkasovsky, M., Herter, P., Voss, B., Wittinghofer, A. Biol. Chem. (2005) [Pubmed]
  17. Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Hsu, S.C., Hazuka, C.D., Roth, R., Foletti, D.L., Heuser, J., Scheller, R.H. Neuron (1998) [Pubmed]
  18. Eavesdropping on the cytoskeleton: progress and controversy in the yeast morphogenesis checkpoint. Keaton, M.A., Lew, D.J. Curr. Opin. Microbiol. (2006) [Pubmed]
  19. The GIN4 family kinase, Cdr2p, acts independently of septins in fission yeast. Morrell, J.L., Nichols, C.B., Gould, K.L. J. Cell. Sci. (2004) [Pubmed]
  20. Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function. Frazier, J.A., Wong, M.L., Longtine, M.S., Pringle, J.R., Mann, M., Mitchison, T.J., Field, C. J. Cell Biol. (1998) [Pubmed]
  21. Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae. Versele, M., Gullbrand, B., Shulewitz, M.J., Cid, V.J., Bahmanyar, S., Chen, R.E., Barth, P., Alber, T., Thorner, J. Mol. Biol. Cell (2004) [Pubmed]
  22. Shs1p: a novel member of septin that interacts with spa2p, involved in polarized growth in saccharomyces cerevisiae. Mino, A., Tanaka, K., Kamei, T., Umikawa, M., Fujiwara, T., Takai, Y. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  23. Functional analysis of the interaction between Afr1p and the Cdc12p septin, two proteins involved in pheromone-induced morphogenesis. Giot, L., Konopka, J.B. Mol. Biol. Cell (1997) [Pubmed]
  24. The kinetochore protein Ndc10p is required for spindle stability and cytokinesis in yeast. Bouck, D.C., Bloom, K.S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  25. Role of a Cdc42p effector pathway in recruitment of the yeast septins to the presumptive bud site. Iwase, M., Luo, J., Nagaraj, S., Longtine, M., Kim, H.B., Haarer, B.K., Caruso, C., Tong, Z., Pringle, J.R., Bi, E. Mol. Biol. Cell (2006) [Pubmed]
  26. Morphogenesis beyond cytokinetic arrest in Saccharomyces cerevisiae. Jiménez, J., Cid, V.J., Cenamor, R., Yuste, M., Molero, G., Nombela, C., Sánchez, M. J. Cell Biol. (1998) [Pubmed]
  27. A novel role for the CBF3 kinetochore-scaffold complex in regulating septin dynamics and cytokinesis. Gillis, A.N., Thomas, S., Hansen, S.D., Kaplan, K.B. J. Cell Biol. (2005) [Pubmed]
  28. Essential function of the polo box of Cdc5 in subcellular localization and induction of cytokinetic structures. Song, S., Grenfell, T.Z., Garfield, S., Erikson, R.L., Lee, K.S. Mol. Cell. Biol. (2000) [Pubmed]
  29. Identification of a developmentally regulated septin and involvement of the septins in spore formation in Saccharomyces cerevisiae. Fares, H., Goetsch, L., Pringle, J.R. J. Cell Biol. (1996) [Pubmed]
  30. Septin-dependent assembly of a cell cycle-regulatory module in Saccharomyces cerevisiae. Longtine, M.S., Theesfeld, C.L., McMillan, J.N., Weaver, E., Pringle, J.R., Lew, D.J. Mol. Cell. Biol. (2000) [Pubmed]
  31. cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. Chang, F., Drubin, D., Nurse, P. J. Cell Biol. (1997) [Pubmed]
  32. Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function. Casamayor, A., Snyder, M. Mol. Cell. Biol. (2003) [Pubmed]
  33. Kcc4 associates with septin proteins of Saccharomyces cerevisiae. Okuzaki, D., Nojima, H. FEBS Lett. (2001) [Pubmed]
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