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Gene Review

SPC42  -  Spc42p

Saccharomyces cerevisiae S288c

Synonyms: Spindle pole body component SPC42, YKL042W, YKL255
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High impact information on SPC42

  • We find that Mlp2p binds directly to Spc110p, Spc42p, and Spc29p, which are three core components of the spindle pole body (SPB), the nuclear envelope-associated yeast spindle organizer [1].
  • A screen for dosage suppressors of the mps1-8 conditional growth phenotype identified the gene encoding the integral SPB component SPC42 [2].
  • We conclude that Mps1p regulates assembly of the integral SPB component Spc42p during SPB duplication [2].
  • Additionally, distinct spots of Ndc1p localization colocalize with a known SPB component, Spc42p [3].
  • Finally, we isolated a complex containing Spc110p, Spc42p, calmodulin and a 35 kDa protein, suggesting that these four proteins interact in the SPB [4].

Biological context of SPC42


Anatomical context of SPC42

  • Taken together, these data suggest that Spc42p forms a polymeric layer at the periphery of the SPB central plaque which has an essential function during SPB duplication and may facilitate attachment of the SPB to the nuclear membrane [7].

Associations of SPC42 with chemical compounds

  • We found that a change to a proline residue in a potential coiled-coil region of Spc42p was responsible for the ts phenotype in at least three alleles, suggesting that formation of the coiled-coil is essential in normal function [7].

Other interactions of SPC42


Analytical, diagnostic and therapeutic context of SPC42

  • Seven temperature-sensitive (ts) mutants in SPC42 were prepared by error-prone PCR [7].


  1. The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly. Niepel, M., Strambio-de-Castillia, C., Fasolo, J., Chait, B.T., Rout, M.P. J. Cell Biol. (2005) [Pubmed]
  2. The yeast protein kinase Mps1p is required for assembly of the integral spindle pole body component Spc42p. Castillo, A.R., Meehl, J.B., Morgan, G., Schutz-Geschwender, A., Winey, M. J. Cell Biol. (2002) [Pubmed]
  3. Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies. Chial, H.J., Rout, M.P., Giddings, T.H., Winey, M. J. Cell Biol. (1998) [Pubmed]
  4. 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]
  5. Cdc28/Cdk1 regulates spindle pole body duplication through phosphorylation of Spc42 and Mps1. Jaspersen, S.L., Huneycutt, B.J., Giddings, T.H., Resing, K.A., Ahn, N.G., Winey, M. Dev. Cell (2004) [Pubmed]
  6. A mutation in SPC42, which encodes a component of the spindle pole body, results in production of two-spored asci in Saccharomyces cerevisiae. Ishihara, S., Hirata, A., Minemura, M., Nogami, S., Ohya, Y. Mol. Genet. Genomics (2001) [Pubmed]
  7. Spc42p: a phosphorylated component of the S. cerevisiae spindle pole body (SPD) with an essential function during SPB duplication. Donaldson, A.D., Kilmartin, J.V. J. Cell Biol. (1996) [Pubmed]
  8. Analysis of a spindle pole body mutant reveals a defect in biorientation and illuminates spindle forces. Yoder, T.J., McElwain, M.A., Francis, S.E., Bagley, J., Muller, E.G., Pak, B., O'Toole, E.T., Winey, M., Davis, T.N. Mol. Biol. Cell (2005) [Pubmed]
  9. Yeast kinetochore microtubule dynamics analyzed by high-resolution three-dimensional microscopy. Dorn, J.F., Jaqaman, K., Rines, D.R., Jelson, G.S., Sorger, P.K., Danuser, G. Biophys. J. (2005) [Pubmed]
  10. 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]
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