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Gene Review

MCK1  -  Mck1p

Saccharomyces cerevisiae S288c

Synonyms: CMS1, Meiosis and centromere regulatory kinase, N0392, Protein kinase MCK1, YNL307C, ...
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High impact information on MCK1

  • This observation indicates that MCK1 is required, independently, for both the activation of IME1 and subsequent ascus maturation [1].
  • We have identified a yeast gene, MCK1, that encodes a positive regulator of meiosis and spore formation [1].
  • This observation is consistent with evidence that MCK1 plays a role in governing centromere function during vegetative growth as well as sporulation [1].
  • The yeast MCK1 gene encodes a protein kinase homolog that activates early meiotic gene expression [1].
  • Increased MCK1 gene dosage accelerates the sporulation program; mck1 mutations cause delayed and decreased levels of sporulation [1].

Biological context of MCK1

  • Co-overexpression of MCK1 suppressed all of the phenotypes associated with PYK1 overexpression [2].
  • The significant homologs are RIM11 and MCK1 that presumably arose from a recent genome duplication followed by a rapid divergence [3].
  • The open reading frame predicts a 375 amino acid polypeptide with a putative protein kinase domain that displays 70% and 39% identity, respectively, to two known yeast proteins, Mds1p and Mck1p [4].
  • Disruption of MCK1 confers a cold-sensitive phenotype, a temperature-sensitive phenotype, and sensitivity to the microtubule-destabilizing drug benomyl and leads to loss of chromosomes during growth on benomyl [5].
  • The yeast gene MCK1 encodes a serine/threonine protein kinase that is thought to function in regulating kinetochore activity and entry into meiosis [5].

Anatomical context of MCK1


Associations of MCK1 with chemical compounds

  • The 42-kDa tyrosine-phosphorylated protein was identified as Mck1, which is a member of the GSK3 family of protein kinases and previously known to be phosphorylated on tyrosine [6].
  • These results suggest that the trehalose-6-phosphate inhibition of hexokinase activity is required for full induction of MCK1 in sporulating yeast cells [7].
  • Since Mck1p is a known serine/threonine protein kinase, this suppression is postulated to be due to Mck1p-catalyzed in vivo phosphorylation of centromere binding proteins [8].
  • Both kinases transmit nutrient signals, but Mck1 transmits additional signals including stress signals such as, temperature, osmotic shock and Ca(2+) [3].
  • The results suggest conformational alterations at the active site of YPK where phosphoryl transfer occurs upon mutation of Thr-298 [9].

Physical interactions of MCK1

  • In medium with a high concentration of Ca2+, Hsl1 was delocalized from the bud neck and destabilized in a manner dependent on both calcineurin and Mck1 [10].

Enzymatic interactions of MCK1


Regulatory relationships of MCK1

  • Suppression of temperature sensitivity by an osmotic stabilizer is also observed in the bul1 bul2 double null mutant, and the temperature sensitivity of the bul1 bul2 double null mutant is suppressed by multiple copies of MCK1 [11].
  • These results indicate that Mck1 negatively regulates pyruvate kinase activity, possibly by direct phosphorylation [2].
  • Mck1p must be catalytically active to inhibit Tpk1p, but Mck1p does not phosphorylate this target [12].

Other interactions of MCK1


Analytical, diagnostic and therapeutic context of MCK1


  1. The yeast MCK1 gene encodes a protein kinase homolog that activates early meiotic gene expression. Neigeborn, L., Mitchell, A.P. Genes Dev. (1991) [Pubmed]
  2. Mck1, a member of the glycogen synthase kinase 3 family of protein kinases, is a negative regulator of pyruvate kinase in the yeast Saccharomyces cerevisiae. Brazill, D.T., Thorner, J., Martin, G.S. J. Bacteriol. (1997) [Pubmed]
  3. The Saccharomyces cerevisiae GSK-3beta homologs. Kassir, Y., Rubin-Bejerano, I., Mandel-Gutfreund, Y. Current drug targets (2006) [Pubmed]
  4. Novel Saccharomyces cerevisiae gene, MRK1, encoding a putative protein kinase with similarity to mammalian glycogen synthase kinase-3 and Drosophila Zeste-White3/Shaggy. Hardy, T.A., Wu, D., Roach, P.J. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  5. MDS1, a dosage suppressor of an mck1 mutant, encodes a putative yeast homolog of glycogen synthase kinase 3. Puziss, J.W., Hardy, T.A., Johnson, R.B., Roach, P.J., Hieter, P. Mol. Cell. Biol. (1994) [Pubmed]
  6. Essential functions of protein tyrosine phosphatases PTP2 and PTP3 and RIM11 tyrosine phosphorylation in Saccharomyces cerevisiae meiosis and sporulation. Zhan, X.L., Hong, Y., Zhu, T., Mitchell, A.P., Deschenes, R.J., Guan, K.L. Mol. Biol. Cell (2000) [Pubmed]
  7. Roles of trehalose phosphate synthase in yeast glycogen metabolism and sporulation. De Silva-Udawatta, M.N., Cannon, J.F. Mol. Microbiol. (2001) [Pubmed]
  8. Overexpression of the yeast MCK1 protein kinase suppresses conditional mutations in centromere-binding protein genes CBF2 and CBF5. Jiang, W., Lim, M.Y., Yoon, H.J., Thorner, J., Martin, G.S., Carbon, J. Mol. Gen. Genet. (1995) [Pubmed]
  9. Monitoring active site alterations upon mutation of yeast pyruvate kinase using 205Tl+ NMR. Susan-Resiga, D., Nowak, T. J. Biol. Chem. (2003) [Pubmed]
  10. GSK-3 kinase Mck1 and calcineurin coordinately mediate Hsl1 down-regulation by Ca2+ in budding yeast. Mizunuma, M., Hirata, D., Miyaoka, R., Miyakawa, T. EMBO J. (2001) [Pubmed]
  11. Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5. Andoh, T., Hirata, Y., Kikuchi, A. Mol. Cell. Biol. (2000) [Pubmed]
  12. Direct and novel regulation of cAMP-dependent protein kinase by Mck1p, a yeast glycogen synthase kinase-3. Rayner, T.F., Gray, J.V., Thorner, J.W. J. Biol. Chem. (2002) [Pubmed]
  13. The dual-specificity protein phosphatase Yvh1p acts upstream of the protein kinase mck1p in promoting spore development in Saccharomyces cerevisiae. Beeser, A.E., Cooper, T.G. J. Bacteriol. (1999) [Pubmed]
  14. Molecular characterization of the yeast meiotic regulatory gene RIM1. Su, S.S., Mitchell, A.P. Nucleic Acids Res. (1993) [Pubmed]
  15. The Kluyveromyces lactis gene KLGSK-3 combines functions which in Saccharomyces cerevisiae are performed by MCK1 and MSD1. Rodríguez-Belmonte, E., González-Siso, I., Cerdán, E. Curr. Genet. (1998) [Pubmed]
  16. Yeast MCK1 protein kinase autophosphorylates at tyrosine and serine but phosphorylates exogenous substrates at serine and threonine. Lim, M.Y., Dailey, D., Martin, G.S., Thorner, J. J. Biol. Chem. (1993) [Pubmed]
  17. Role of lysine 240 in the mechanism of yeast pyruvate kinase catalysis. Bollenbach, T.J., Mesecar, A.D., Nowak, T. Biochemistry (1999) [Pubmed]
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