Carbonyl cyanide m-chlorophenylhydrazone induced calcium signaling and activation of plasma membrane H(+)-ATPase in the yeast Saccharomyces cerevisiae

FEMS Yeast Res. 2008 Jun;8(4):622-30. doi: 10.1111/j.1567-1364.2008.00380.x. Epub 2008 Apr 8.

Abstract

The plasma membrane H(+)-ATPase from Saccharomyces cerevisiae is an enzyme that plays a very important role in the yeast physiology. The addition of protonophores, such as 2,4-dinitrophenol (DNP) and carbonyl cyanide m-chlorophenylhydrazone (CCCP), also triggers a clear in vivo activation of this enzyme. Here, we demonstrate that CCCP-induced activation of the plasma membrane H(+)-ATPase shares some similarities with the sugar-induced activation of the enzyme. Phospholipase C and protein kinase C activities are essential for this activation process while Gpa2p, a G protein involved in the glucose-induced activation of the ATPase, is not required. CCCP also induces a phospholipase C-dependent increase in intracellular calcium. Moreover, we show that the availability of extracellular calcium is required for CCCP stimulation of H(+)-ATPase, suggesting a possible connection between calcium signaling and activation of ATPase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium / analysis
  • Calcium Signaling / drug effects*
  • Carbonyl Cyanide m-Chlorophenyl Hydrazone / analogs & derivatives*
  • Carbonyl Cyanide m-Chlorophenyl Hydrazone / pharmacology
  • Cell Membrane / enzymology*
  • Cytosol / chemistry
  • GTP-Binding Protein alpha Subunits / metabolism
  • Ionophores / pharmacology*
  • Protein Kinase C / metabolism
  • Proton-Translocating ATPases / metabolism*
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / metabolism
  • Type C Phospholipases / metabolism

Substances

  • GTP-Binding Protein alpha Subunits
  • Ionophores
  • Saccharomyces cerevisiae Proteins
  • Carbonyl Cyanide m-Chlorophenyl Hydrazone
  • Protein Kinase C
  • Type C Phospholipases
  • Proton-Translocating ATPases
  • Gpa2 protein, S cerevisiae
  • Calcium