Open AccessCarbonyl cyanide m ‐chlorophenylhydrazone induced calcium signaling and activation of plasma membrane H + ‐ATPase in the yeast Saccharomyces cerevisiae
Author(s) -
Pereira Michele B.P.,
Tisi Renata,
Fietto Luciano G.,
Cardoso Anamaria S.,
França Mônica M.,
Carvalho Fernanda M.,
Trópia Maria José M.,
Martegani Enzo,
Castro Ieso M.,
Brandão Rogelio L.
Publication year - 2008
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2008.00380.x
Subject(s) - atpase , biology , phospholipase , plasma membrane ca2+ atpase , biochemistry , phospholipase c , saccharomyces cerevisiae , calcium atpase , calcium , extracellular , enzyme , phospholipase d , microbiology and biotechnology , yeast , chemistry , organic chemistry
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.