cAMP- and RAS-independent nutritional regulation of plasma-membrane H+-ATPase activity in Saccharomyces cerevisiae.
The plasma-membrane ATPase of Saccharomyces cerevisiae is a proton pump whose activity, essential fro proliferation, is subject to regulation by nutritional signals. The previous finding that the CDC25 gene product is required for the glucose-induced H+-ATPase activation suggested that H+-ATPase activity is regulated by cAMP. Analysis of starvation-induced inactivation and glucose-induced activation of the H+-ATPase in mutants affected in activity of the RAS proteins, adenylyl cyclase or cAMP-dependent protein kinase showed that nutritional regulation of H+-ATPase activity does not depend directly on any of these factors. We conclude that adenlyl cyclase does not mediate all nutritional responses. This also indicates that the specific CDC25 requirement for the glucose-induced activation of the H+-ATPase identifies a new function for the CDC25 gene product, a function that appears to be independent of CDC25-mediated modulation of the RAS/adenylyl cyclase/cAMP pathway.
Mazón
M J
MJ
Instituto de Investigaciones del Consejo Superior, Madrid
Behrens
M M
MM
Portillo
F
F
Piñón
R
R
D018797:Cell Cycle Proteins; D002462:Cell Membrane / Q000201:enzymology*; D000242:Cyclic AMP / Q000502:physiology; D005656:Fungal Proteins / Q000378:metabolism*; D005947:Glucose / Q000494:pharmacology; D011494:Protein Kinases / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D020666:ras-GRF1
D018797:Cell Cycle Proteins; D005656:Fungal Proteins; D020666:ras-GRF1; D000242:Cyclic AMP; D011494:Protein Kinases; D006180:Proton-Translocating ATPases; D005947:Glucose