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Gene Review

TUB4  -  Tub4p

Saccharomyces cerevisiae S288c

Synonyms: Gamma-tubulin, L8167.21, Tubulin gamma chain, YLR212C
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Disease relevance of TUB4


High impact information on TUB4


Biological context of TUB4


Anatomical context of TUB4

  • Study of a temperature sensitive tub4-1 allele revealed that TUB4 has essential functions in microtubule organization [8].
  • Finally, we report the identification of a large 22 S Tub4p complex in yeast extract that contains multimers of Spc97p similar to gamma-tubulin ring complexes found in higher eukaryotic cells [7].
  • These results suggest that different components of MTOCs act as receptors for gamma-tubulin complexes and that they are essential for the function of MTOCs [10].
  • Homologues of Spc97p and Spc98p have been identified from yeast to mammalian cells and these are also part of gamma-tubulin complexes, suggesting that these related proteins may also interact with GTBPs at the centrosome [11].
  • Loss of function of the gamma-tubulin gene by RNAi induces a strong polyploidization of mitotic germ cells and embryos, but does not affect meiosis and pronuclear migration [12].

Associations of TUB4 with chemical compounds

  • Sucrose gradient sedimentation of the cytosolic fraction and immunoprecipitation experiments demonstrate that both gamma-tubulin and HsSpc98p are in the same complex [13].
  • Alanine substitution for any one of these phosphorylated residues, in conjunction with an alanine substitution at residue Ser(36), is lethal in combination with alleles of SPC97, which encodes a component of the Tub4p complex [14].

Physical interactions of TUB4


Other interactions of TUB4


Analytical, diagnostic and therapeutic context of TUB4


  1. The spindle pole body component Spc98p interacts with the gamma-tubulin-like Tub4p of Saccharomyces cerevisiae at the sites of microtubule attachment. Geissler, S., Pereira, G., Spang, A., Knop, M., Souès, S., Kilmartin, J., Schiebel, E. EMBO J. (1996) [Pubmed]
  2. Gamma-tubulin is a centrosomal protein required for cell cycle-dependent microtubule nucleation. Joshi, H.C., Palacios, M.J., McNamara, L., Cleveland, D.W. Nature (1992) [Pubmed]
  3. gamma-tubulin complexes: binding to the centrosome, regulation and microtubule nucleation. Schiebel, E. Curr. Opin. Cell Biol. (2000) [Pubmed]
  4. Regulating microtubule properties by modifying their organizing minus ends. Usui, T., Schiebel, E. Mol. Cell (2001) [Pubmed]
  5. Nud1p links astral microtubule organization and the control of exit from mitosis. Gruneberg, U., Campbell, K., Simpson, C., Grindlay, J., Schiebel, E. EMBO J. (2000) [Pubmed]
  6. The spindle pole body component Spc97p interacts with the gamma-tubulin of Saccharomyces cerevisiae and functions in microtubule organization and spindle pole body duplication. Knop, M., Pereira, G., Geissler, S., Grein, K., Schiebel, E. EMBO J. (1997) [Pubmed]
  7. Reconstitution and characterization of budding yeast gamma-tubulin complex. Vinh, D.B., Kern, J.W., Hancock, W.O., Howard, J., Davis, T.N. Mol. Biol. Cell (2002) [Pubmed]
  8. gamma-Tubulin-like Tub4p of Saccharomyces cerevisiae is associated with the spindle pole body substructures that organize microtubules and is required for mitotic spindle formation. Spang, A., Geissler, S., Grein, K., Schiebel, E. J. Cell Biol. (1996) [Pubmed]
  9. A highly divergent gamma-tubulin gene is essential for cell growth and proper microtubule organization in Saccharomyces cerevisiae. Sobel, S.G., Snyder, M. J. Cell Biol. (1995) [Pubmed]
  10. Receptors determine the cellular localization of a gamma-tubulin complex and thereby the site of microtubule formation. Knop, M., Schiebel, E. EMBO J. (1998) [Pubmed]
  11. Microtubule organization by the budding yeast spindle pole body. Knop, M., Pereira, G., Schiebel, E. Biol. Cell (1999) [Pubmed]
  12. Identification and characterization of Caenorhabditis elegans gamma-tubulin in dividing cells and differentiated tissues. Bobinnec, Y., Fukuda, M., Nishida, E. J. Cell. Sci. (2000) [Pubmed]
  13. Characterization of the human homologue of the yeast spc98p and its association with gamma-tubulin. Tassin, A.M., Celati, C., Moudjou, M., Bornens, M. J. Cell Biol. (1998) [Pubmed]
  14. Yeast Mps1p phosphorylates the spindle pole component Spc110p in the N-terminal domain. Friedman, D.B., Kern, J.W., Huneycutt, B.J., Vinh, D.B., Crawford, D.K., Steiner, E., Scheiltz, D., Yates, J., Resing, K.A., Ahn, N.G., Winey, M., Davis, T.N. J. Biol. Chem. (2001) [Pubmed]
  15. Loss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae. Oka, M., Nakai, M., Endo, T., Lim, C.R., Kimata, Y., Kohno, K. J. Biol. Chem. (1998) [Pubmed]
  16. A genetic analysis of interactions with Spc110p reveals distinct functions of Spc97p and Spc98p, components of the yeast gamma-tubulin complex. Nguyen, T., Vinh, D.B., Crawford, D.K., Davis, T.N. Mol. Biol. Cell (1998) [Pubmed]
  17. Genetic and biochemical interactions between the Arp2/3 complex, Cmd1p, casein kinase II, and Tub4p in yeast. Schaerer-Brodbeck, C., Riezman, H. FEMS Yeast Res. (2003) [Pubmed]
  18. Gamma-tubulin complexes and their interaction with microtubule-organizing centers. Wiese, C., Zheng, Y. Curr. Opin. Struct. Biol. (1999) [Pubmed]
  19. Paxillin localizes to the lymphocyte microtubule organizing center and associates with the microtubule cytoskeleton. Herreros, L., Rodríguez-Fernandez, J.L., Brown, M.C., Alonso-Lebrero, J.L., Cabañas, C., Sánchez-Madrid, F., Longo, N., Turner, C.E., Sánchez-Mateos, P. J. Biol. Chem. (2000) [Pubmed]
  20. Molecular and structural characterization of the spindle pole bodies in the fission yeast Schizosaccharomyces japonicus var japonicus. Horio, T., Kimura, N., Basaki, A., Tanaka, Y., Noguchi, T., Akashi, T., Tanaka, K. Yeast (2002) [Pubmed]
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