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Gene Review

PMC1  -  calcium-transporting ATPase PMC1

Saccharomyces cerevisiae S288c

Synonyms: Calcium-transporting ATPase 2, Vacuolar Ca(2+)-ATPase, YGL006W
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Disease relevance of PMC1

  • Instead, the prz1-null cells showed hypersensitivity to Ca(2+), consistent with a dramatic decrease in transcription of Pmc1 Ca(2+) pump [1].
  • We also show that suppression of calcium toxicity by the calcium pumps Pmr1p and Pmc1p is restricted only to the subset of mutants defective in vacuole morphology [2].

High impact information on PMC1

  • In addition, we found that the calcineurin-dependent transcriptional regulation of PMR2 and PMC1 required CRZ1 [3].
  • A second Ca2+ ATPase homolog encoded by the PMR1 gene acts together with PMC1 to prevent lethal activation of calcineurin even in standard (low Ca2+) conditions [4].
  • The PMC1 gene of Saccharomyces cerevisiae encodes a vacuole membrane protein that is 40% identical to the plasma membrane Ca2+ ATPases (PMCAs) of mammalian cells [4].
  • Calcineurin-dependent growth control in Saccharomyces cerevisiae mutants lacking PMC1, a homolog of plasma membrane Ca2+ ATPases [4].
  • Mutations in calcineurin A or B subunits or the inhibitory compounds FK506 and cyclosporin A restore growth of pmc1 mutants in high Ca2+ media [4].

Biological context of PMC1


Anatomical context of PMC1

  • We also show that Snf3p could be involved in the control of Pmc1p activity that would regulate the calcium availability in the cytosol [7].

Associations of PMC1 with chemical compounds

  • ACA4 and PMC1, the yeast vacuolar Ca(2+)-ATPase, conferred protection against osmotic stress such as high NaCl, KCl, and mannitol when expressed in the K616 strain [8].
  • However, PMC1 did not play a direct role in the survival of C. albicans when exposed to fluconazole [9].
  • We conclude that Nyv1p can interact physically with Pmc1p and inhibit its Ca(2+) transport activity in the vacuole membrane [10].
  • These observations suggest that Li+ inhibition of phosphoglucomutase results in an increased glucose-1-phosphate-to-glucose-6-phosphate ratio, which results in an accelerated rate of vacuolar Ca2+ uptake via the Ca2+-ATPase Pmc1p [11].

Other interactions of PMC1

  • In the yeast Saccharomyces cerevisiae, the Golgi PMR1 Ca(2+)-ATPase and the vacuole PMC1 Ca(2+)-ATPase function together in Ca2+ sequestration and Ca2+ tolerance [5].
  • Activities of VCX1 and PMC1 help to control cytosolic free Ca2+ concentrations because their function can decrease pmc1::lacZ induction by calcineurin [12].
  • Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p [10].


  1. Zinc finger protein Prz1 regulates Ca2+ but not Cl- homeostasis in fission yeast. Identification of distinct branches of calcineurin signaling pathway in fission yeast. Hirayama, S., Sugiura, R., Lu, Y., Maeda, T., Kawagishi, K., Yokoyama, M., Tohda, H., Giga-Hama, Y., Shuntoh, H., Kuno, T. J. Biol. Chem. (2003) [Pubmed]
  2. Multiple functions of the vacuolar sorting protein Ccz1p in Saccharomyces cerevisiae. Hoffman-Sommer, M., Migdalski, A., Rytka, J., Kucharczyk, R. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  3. Calcineurin acts through the CRZ1/TCN1-encoded transcription factor to regulate gene expression in yeast. Stathopoulos, A.M., Cyert, M.S. Genes Dev. (1997) [Pubmed]
  4. Calcineurin-dependent growth control in Saccharomyces cerevisiae mutants lacking PMC1, a homolog of plasma membrane Ca2+ ATPases. Cunningham, K.W., Fink, G.R. J. Cell Biol. (1994) [Pubmed]
  5. Rabbit sarcoplasmic reticulum Ca(2+)-ATPase replaces yeast PMC1 and PMR1 Ca(2+)-ATPases for cell viability and calcineurin-dependent regulation of calcium tolerance. Degand, I., Catty, P., Talla, E., Thinès-Sempoux, D., de Kerchove d'Exaerde, A., Goffeau, A., Ghislain, M. Mol. Microbiol. (1999) [Pubmed]
  6. The Ca2+ homeostasis defects in a pgm2Delta strain of Saccharomyces cerevisiae are caused by excessive vacuolar Ca2+ uptake mediated by the Ca2+-ATPase Pmc1p. Aiello, D.P., Fu, L., Miseta, A., Sipos, K., Bedwell, D.M. J. Biol. Chem. (2004) [Pubmed]
  7. Calcium signaling and sugar-induced activation of plasma membrane H(+)-ATPase in Saccharomyces cerevisiae cells. Trópia, M.J., Cardoso, A.S., Tisi, R., Fietto, L.G., Fietto, J.L., Martegani, E., Castro, I.M., Brandão, R.L. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  8. The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that improves salt tolerance in yeast. Geisler, M., Frangne, N., Gomès, E., Martinoia, E., Palmgren, M.G. Plant Physiol. (2000) [Pubmed]
  9. Calcineurin A of Candida albicans: involvement in antifungal tolerance, cell morphogenesis and virulence. Sanglard, D., Ischer, F., Marchetti, O., Entenza, J., Bille, J. Mol. Microbiol. (2003) [Pubmed]
  10. Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p. Takita, Y., Engstrom, L., Ungermann, C., Cunningham, K.W. J. Biol. Chem. (2001) [Pubmed]
  11. Inhibition of phosphoglucomutase activity by lithium alters cellular calcium homeostasis and signaling in Saccharomyces cerevisiae. Csutora, P., Strassz, A., Boldizsár, F., Németh, P., Sipos, K., Aiello, D.P., Bedwell, D.M., Miseta, A. Am. J. Physiol., Cell Physiol. (2005) [Pubmed]
  12. Calcineurin inhibits VCX1-dependent H+/Ca2+ exchange and induces Ca2+ ATPases in Saccharomyces cerevisiae. Cunningham, K.W., Fink, G.R. Mol. Cell. Biol. (1996) [Pubmed]
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