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Gene Review

SPC110  -  Spc110p

Saccharomyces cerevisiae S288c

Synonyms: D9476.3, Extragenic suppressor of CMD1-1 mutant protein 1, NUF1, Nuclear filament-related protein 1, Spindle pole body component 110, ...
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High impact information on SPC110


Biological context of SPC110

  • Deletion of HCM1 does not affect the basal level of SPC110 transcription, but reduces the induction that occurs late in G1 of the cell cycle [5].
  • The promoter of SPC110 contains a match to the consensus binding site [5].
  • Nuf1p/Spc110p, one of the essential targets, is a spindle pole body component that is required for proper mitosis [6].
  • Additionally, these mutants displayed characteristic mitotic defects: an increased ratio of artificial chromosome loss, which could be suppressed by the CaM-independent dominant allele of NUF1, and aberrant microtubule structures [6].
  • However, the interaction was restored in a heterozygous diploid of the two cmd1 alleles, suggesting that intragenic complementation between these cmd1 alleles occurs by a novel mechanism, whereby co-presence of both mutant proteins rescues the interaction with Nuf1p [6].

Anatomical context of SPC110


Associations of SPC110 with chemical compounds

  • Ser(60), Thr(64), and Thr(68) are the major sites in Spc110p phosphorylated by Mps1p in vitro, and alanine substitution at these sites abolishes the mitosis-specific isoform in vivo [8].

Physical interactions of SPC110

  • Immunoprecipitation analysis showed that two cmd1 mutations belonging to two distinct intragenic complementation groups had the most severely impaired complex formation with Nuf1p at the restrictive temperature [6].
  • Cdc31p was also able to bind to the carboxy terminus of Nuflp/Spc110p, another component of the SPB (Kilmartin, J. V., S. L. Dyos, D. Kershaw, and J. T. Finch. 1993. J. Cell Biol. 123:1175-1184) [10].
  • We tested whether binding of the recombinant Tub4p complex to the spindle pole body docking protein Spc110p affects its nucleating activity [11].

Regulatory relationships of SPC110

  • The temperature-sensitive growth of these cmd1 mutants was suppressed by a CaM-independent dominant allele of NUF1 [6].

Other interactions of SPC110

  • Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication [12].
  • Together, these studies provide evidence that Spc110p directly links the Tub4p complex to the SPB [7].
  • In contrast, the spc97 alleles are synthetic lethal with spc110 alleles that encode mutations in either the N terminus or the C terminus [7].
  • We also found that mutations in SPC110, which encodes a major SPB component, showed genetic interactions with both CDC31 and the PKC1 pathway [13].
  • In support of the model that the PKC1 pathway regulates SPB duplication, one of the phosphorylated forms of Spc110p was absent in pkc1 and mpk1Delta mutants [13].

Analytical, diagnostic and therapeutic context of SPC110

  • Using the two-hybrid assay, we show that the interactions of Spc110p with Spc97p and Spc98p are not equivalent [7].
  • In addition, immunofluorescence results indicate that mammalian cells contain a NUF1-related nuclear protein [14].
  • Sequence analysis of the NUF1 gene predicts a protein 945 amino acids in length that contains three domains: a large 627 residue central domain predicted to form a coiled-coil structure flanked by nonhelical amino-terminal and carboxy-terminal regions [14].
  • Antibodies to NUF1 fusion proteins were generated, and affinity-purified antibodies were used for immunoblot analysis and indirect immunofluorescence localization [14].
  • Asynchronous wild-type cultures contain two electrophoretically distinct isoforms of Spc110p as detected by Western blot analysis, suggesting that Spc110p is modified in vivo [15].


  1. 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]
  2. Spc98p and Spc97p of the yeast gamma-tubulin complex mediate binding to the spindle pole body via their interaction with Spc110p. Knop, M., Schiebel, E. EMBO J. (1997) [Pubmed]
  3. Role of calmodulin and Spc110p interaction in the proper assembly of spindle pole body compenents. Sundberg, H.A., Goetsch, L., Byers, B., Davis, T.N. J. Cell Biol. (1996) [Pubmed]
  4. Spc110p: assembly properties and role in the connection of nuclear microtubules to the yeast spindle pole body. Kilmartin, J.V., Goh, P.Y. EMBO J. (1996) [Pubmed]
  5. The fork head transcription factor Hcm1p participates in the regulation of SPC110, which encodes the calmodulin-binding protein in the yeast spindle pole body. Zhu, G., Davis, T.N. Biochim. Biophys. Acta (1998) [Pubmed]
  6. A novel mechanism of intragenic complementation between Phe to Ala calmodulin mutations. Okano, H., Asakawa, M., Ohya, Y. J. Biochem. (2004) [Pubmed]
  7. 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]
  8. 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]
  9. Identification of a human centrosomal calmodulin-binding protein that shares homology with pericentrin. Flory, M.R., Moser, M.J., Monnat, R.J., Davis, T.N. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  10. The Cdc31p-binding protein Kar1p is a component of the half bridge of the yeast spindle pole body. Spang, A., Courtney, I., Grein, K., Matzner, M., Schiebel, E. J. Cell Biol. (1995) [Pubmed]
  11. 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]
  12. Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication. Elliott, S., Knop, M., Schlenstedt, G., Schiebel, E. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  13. Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes. Khalfan, W., Ivanovska, I., Rose, M.D. Genetics (2000) [Pubmed]
  14. The NUF1 gene encodes an essential coiled-coil related protein that is a potential component of the yeast nucleoskeleton. Mirzayan, C., Copeland, C.S., Snyder, M. J. Cell Biol. (1992) [Pubmed]
  15. The 110-kD spindle pole body component of Saccharomyces cerevisiae is a phosphoprotein that is modified in a cell cycle-dependent manner. Friedman, D.B., Sundberg, H.A., Huang, E.Y., Davis, T.N. J. Cell Biol. (1996) [Pubmed]
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