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CDC11  -  septin CDC11

Saccharomyces cerevisiae S288c

Synonyms: Cell division control protein 11, J1833, PSL9, YJR076C
 
 
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High impact information on CDC11

  • The cytokinesis activity is localized to a centriolin domain that shares homology with Nud1p and Cdc11p, budding and fission yeast proteins that anchor regulatory pathways involved in progression through the late stages of mitosis [1].
  • We have identified four major SUMO attachment-site lysine residues in Cdc3, one in Cdc11, and two in Shs1, all within the consensus sequence (IVL)KX(ED) [2].
  • To investigate the relationship between these filaments and the neck filaments, we purified septin complexes from cells deleted for CDC10 or CDC11 [3].
  • Immunofluorescence observations suggest that Spr3p, Cdc3p, and Cdc11p are localized to the leading edges of the membrane sacs that form near the spindle-pole bodies and gradually extend to engulf the nuclear lobes that contain the haploid chromosome sets, thus forming the spores [4].
  • In addition, a haploid cdc11 mutant loses its axial-budding pattern upon shift to restrictive temperature [5].
 

Biological context of CDC11

  • In cultures started with unbudded cells, an inhibitor of Chs3p activity, nikkomycin Z, aggravated the abnormalities of cla4 and cdc11 mutants and gave rise to enlarged necks at the mother-bud junction, leading to cell death [6].
  • Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC11 gene product and the timing of events at the budding site [7].
  • The YUH1 locus is located approximately 140 kb from the right telomere of chromosome X, and genetically maps 3.6 cM distal to cdc11 [8].
  • It localizes to the spindle pole body at all stages of the cell cycle, in a sid4p-dependent manner, and cdc11p is required for the localization of all the known SIN components, except sid4p, to the SPB [9].
  • Cdc11p is a phosphoprotein, which becomes hyperphosphorylated during anaphase [9].
 

Anatomical context of CDC11

  • Surprisingly, most preparations of affinity purified Cdc11p-specific antibodies also stained the nuclear and cytoplasmic microtubules [7].
  • Cdc11p also localizes to regions of cell-wall reorganization in mating cells and in cells responding to purified mating pheromone [7].
 

Physical interactions of CDC11

  • In addition, Cdc11 forms a stoichiometric complex with Cdc12, independent of its CTE [10].
  • Two-hybrid, in vitro binding, and protein-localization studies suggest that Bni5p interacts with the N-terminal domain of Cdc11p, which also appears to be sufficient for the localization of Cdc11p, its interaction with other septins, and other critical aspects of its function [11].
 

Other interactions of CDC11

  • Deletion of SPR3 does not prevent the localization of Cdc3p and Cdc11p, but these proteins appear to be less well organized, and the intensity of their staining is reduced [4].
  • Cdc11p and actin both localize to the budding site well in advance of bud emergence and at approximately the same time, and both proteins also remain localized at the old budding site for some time after cytokinesis [7].
  • The gene for SOD-1 (SOD1) was physically mapped by Southern blot to restriction fragments containing CDC11. scd1 failed to complement a complete deletion of SOD1 [12].
  • We show that Cdc11, one of the septins, is delocalised in the mutant, indicating that septin localisation is partly controlled by Elm1 [13].
  • The HAM1 gene was localized on the right arm of chromosome X between cdc8 and cdc11 [14].
 

Analytical, diagnostic and therapeutic context of CDC11

  • For example, the Schizosaccharomyces pombe septation-initiation network (SIN), which is responsible for initiating actomyosin ring constriction and septation, is assembled at the SPB through its two scaffolding components, Sid4 and Cdc11 [15].

References

  1. A novel human protein of the maternal centriole is required for the final stages of cytokinesis and entry into S phase. Gromley, A., Jurczyk, A., Sillibourne, J., Halilovic, E., Mogensen, M., Groisman, I., Blomberg, M., Doxsey, S. J. Cell Biol. (2003) [Pubmed]
  2. Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. Johnson, E.S., Blobel, G. J. Cell Biol. (1999) [Pubmed]
  3. 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]
  4. 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]
  5. Role of Bud3p in producing the axial budding pattern of yeast. Chant, J., Mischke, M., Mitchell, E., Herskowitz, I., Pringle, J.R. J. Cell Biol. (1995) [Pubmed]
  6. Septins, under Cla4p regulation, and the chitin ring are required for neck integrity in budding yeast. Schmidt, M., Varma, A., Drgon, T., Bowers, B., Cabib, E. Mol. Biol. Cell (2003) [Pubmed]
  7. Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC11 gene product and the timing of events at the budding site. Ford, S.K., Pringle, J.R. Dev. Genet. (1991) [Pubmed]
  8. The use of random-breakage mapping to locate the genes APN1 and YUH1 in the Saccharomyces genome, and to determine gene order near the left end of chromosome XI. Game, J., Bell, M., Ramotar, D., Miller, H. Yeast (1994) [Pubmed]
  9. S. pombe cdc11p, together with sid4p, provides an anchor for septation initiation network proteins on the spindle pole body. Krapp, A., Schmidt, S., Cano, E., Simanis, V. Curr. Biol. (2001) [Pubmed]
  10. 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]
  11. Bni5p, a septin-interacting protein, is required for normal septin function and cytokinesis in Saccharomyces cerevisiae. Lee, P.R., Song, S., Ro, H.S., Park, C.J., Lippincott, J., Li, R., Pringle, J.R., De Virgilio, C., Longtine, M.S., Lee, K.S. Mol. Cell. Biol. (2002) [Pubmed]
  12. Genetic and biochemical characterization of Cu,Zn superoxide dismutase mutants in Saccharomyces cerevisiae. Chang, E.C., Crawford, B.F., Hong, Z., Bilinski, T., Kosman, D.J. J. Biol. Chem. (1991) [Pubmed]
  13. Regulation of cytokinesis by the Elm1 protein kinase in Saccharomyces cerevisiae. Bouquin, N., Barral, Y., Courbeyrette, R., Blondel, M., Snyder, M., Mann, C. J. Cell. Sci. (2000) [Pubmed]
  14. HAM1, the gene controlling 6-N-hydroxylaminopurine sensitivity and mutagenesis in the yeast Saccharomyces cerevisiae. Noskov, V.N., Staak, K., Shcherbakova, P.V., Kozmin, S.G., Negishi, K., Ono, B.C., Hayatsu, H., Pavlov, Y.I. Yeast (1996) [Pubmed]
  15. Ppc89 links multiple proteins, including the septation initiation network, to the core of the fission yeast spindle-pole body. Rosenberg, J.A., Tomlin, G.C., McDonald, W.H., Snydsman, B.E., Muller, E.G., Yates, J.R., Gould, K.L. Mol. Biol. Cell (2006) [Pubmed]
 
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