HOR7, a multicopy suppressor of the Ca2+-induced growth defect in sphingolipid mannosyltransferase-deficient yeast

J Biol Chem. 2004 Aug 27;279(35):36390-6. doi: 10.1074/jbc.M406197200. Epub 2004 Jun 18.

Abstract

Yeast mutants defective in sphingolipid mannosylation accumulate inositol phosphorylceramide C (IPC-C), which renders cells Ca(2+)-sensitive. A screen for loss of function suppressors of the Ca(2+)-sensitive phenotype previously led to the identification of numerous genes involved in IPC-C synthesis. To better understand the molecular basis of the Ca(2+)-induced growth defect in IPC-C-overaccumulating cells, we searched for genes whose overexpression restored Ca(2+) tolerance in a mutant lacking the IPC mannosyltransferases Csg1p and Csh1p. Here we report the isolation of HOR7 as a multicopy suppressor of the Ca(2+)-sensitive phenotype of Deltacsg1Deltacsh1 cells. HOR7 belongs to a group of hyperosmolarity-responsive genes and encodes a small (59-residue) type I membrane protein that localizes at the plasma membrane. Hor7p is not required for high Ca(2+) or Na(+) tolerance. Instead, we find that Hor7p-overproducing cells display an increased resistance to high salt, sensitivity to low pH, and a reduced uptake of methylammonium, an indicator of the plasma membrane potential. These phenotypes are induced through a mechanism independent of the plasma membrane H(+)-ATPase, Pma1p. Our findings suggest that induction of Hor7p causes a depolarization of the plasma membrane that may counteract a Ca(2+)-induced influx of toxic cations in IPC-C-overaccumulating cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Amino Acid Sequence
  • Blotting, Western
  • Calcium / metabolism*
  • Cell Division
  • Cell Membrane / enzymology
  • Cell Membrane / metabolism
  • Fungal Proteins / metabolism
  • Glycosyltransferases
  • Hydrogen-Ion Concentration
  • Mannosyltransferases / metabolism*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology*
  • Methylamines / chemistry
  • Methylamines / pharmacokinetics
  • Microscopy, Fluorescence
  • Models, Biological
  • Models, Genetic
  • Molecular Sequence Data
  • Phenotype
  • Plasmids / metabolism
  • Protein Structure, Tertiary
  • Proton-Translocating ATPases / metabolism
  • Repressor Proteins / metabolism
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Saccharomyces cerevisiae Proteins / physiology*
  • Signal Transduction
  • Sodium / chemistry
  • Sphingolipids / metabolism*
  • Subcellular Fractions / metabolism
  • Time Factors

Substances

  • CSH1 protein, Candida albicans
  • Fungal Proteins
  • HOR7 protein, S cerevisiae
  • Membrane Proteins
  • Methylamines
  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
  • Sphingolipids
  • Sodium
  • methylamine
  • Glycosyltransferases
  • SUR1 protein, S cerevisiae
  • Mannosyltransferases
  • Adenosine Triphosphatases
  • PMA1 protein, S cerevisiae
  • Proton-Translocating ATPases
  • Calcium