cAMP- and RAS-independent Nutritional Regulation of Plasma-membrane H+-ATPase Activity in Saccharomyces cerevisiae
- 1 June 1989
- journal article
- research article
- Published by Microbiology Society in Microbiology
- Vol. 135 (6) , 1453-1460
- https://doi.org/10.1099/00221287-135-6-1453
Abstract
The plasma-membrane ATPase of Saccharomyces cerevisiae is a proton pump whose activity, essential for 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 adenylyl 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.This publication has 19 references indexed in Scilit:
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