The Ca2+ homeostasis defects in a pgm2Delta strain of Saccharomyces cerevisiae are caused by excessive vacuolar Ca2+ uptake mediated by the Ca2+-ATPase Pmc1p

J Biol Chem. 2004 Sep 10;279(37):38495-502. doi: 10.1074/jbc.M400833200. Epub 2004 Jul 13.

Abstract

Loss of the major isoform of phosphoglucomutase (PGM) causes an accumulation of glucose 1-phosphate when yeast cells are grown with galactose as the carbon and energy source. Remarkably, the pgm2Delta strain also exhibits a severe imbalance in intracellular Ca(2+) homeostasis when grown under these conditions. In the present study, we examined how the pgm2Delta mutation alters yeast Ca(2+) homeostasis in greater detail. We found that a shift from glucose to galactose as the carbon source resulted in a 2-fold increase in the rate of cellular Ca(2+) uptake in wild-type cells, whereas Ca(2+) uptake increased 8-fold in the pgm2Delta mutant. Disruption of the PMC1 gene, which encodes the vacuolar Ca(2+)-ATPase Pmc1p, suppressed the Ca(2+)-related phenotypes observed in the pgm2Delta strain. This suggests that excessive vacuolar Ca(2+) uptake is tightly coupled to these defects in Ca(2+) homeostasis. An in vitro assay designed to measure Ca(2+) sequestration into intracellular compartments confirmed that the pgm2Delta mutant contained a higher level of Pmc1p-dependent Ca(2+) transport activity than the wild-type strain. We found that this increased rate of vacuolar Ca(2+) uptake also coincided with a large induction of the unfolded protein response in the pgm2Delta mutant, suggesting that Ca(2+) uptake into the endoplasmic reticulum compartment was reduced. These results indicate that the excessive Ca(2+) uptake and accumulation previously shown to be associated with the pgm2Delta mutation are due to a severe imbalance in the distribution of cellular Ca(2+) into different intracellular compartments.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Calcium / chemistry
  • Calcium / metabolism*
  • Calcium-Transporting ATPases / metabolism*
  • Carbon / chemistry
  • Cell Membrane / metabolism
  • Culture Media / pharmacology
  • Endoplasmic Reticulum / metabolism
  • Galactose / metabolism
  • Glucose / metabolism
  • Glucose-6-Phosphate / metabolism
  • Glucosephosphates / metabolism
  • Manganese / chemistry
  • Models, Biological
  • Mutation
  • Phosphoglucomutase / genetics*
  • Plasma Membrane Calcium-Transporting ATPases
  • Plasmids / metabolism
  • Protein Isoforms
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Subcellular Fractions / metabolism
  • beta-Galactosidase / metabolism

Substances

  • Culture Media
  • Glucosephosphates
  • PMC1 protein, S cerevisiae
  • Protein Isoforms
  • Saccharomyces cerevisiae Proteins
  • Manganese
  • Glucose-6-Phosphate
  • Carbon
  • glucose-1-phosphate
  • beta-Galactosidase
  • Plasma Membrane Calcium-Transporting ATPases
  • Phosphoglucomutase
  • Calcium-Transporting ATPases
  • Glucose
  • Calcium
  • Galactose