cAMP- and RAS-independent nutritional regulation of plasma-membrane H+-ATPase activity in Saccharomyces cerevisiae

• Published in: Journal of general microbiology Vol. 135; no. 6; pp. 1453 - 1460
• Main Authors: Mazon, M.J, Behrens, M.M, Portillo, F, Pinon, R
• Format: Journal Article
• Language: English
• Published: London Soc General Microbiol 01.06.1989; New York, NY Cambridge University Press
• Subjects: adenosinetriphosphatase; Biological and medical sciences; Cell Cycle Proteins; Cell Membrane - enzymology; cyclic AMP; Cyclic AMP - physiology; Fundamental and applied biological sciences. Psychology; Fungal Proteins - metabolism; Glucose - pharmacology; Growth, nutrition, metabolism, transports, enzymes. Molecular biology; Microbiology; Mycology; nutrition research; plasma membrane; Protein Kinases - metabolism; Proton-Translocating ATPases - metabolism; ras-GRF1; Saccharomyces cerevisiae; Saccharomyces cerevisiae - enzymology; Yeast; Nutrition; Enzyme; Gene product; Cyclic AMP; F0F1-ATPase; Environmental factor; Glucose; Fungi; Adenylate cyclase; Regulation(control); Protein kinase; Ascomycetes; Mutation; Saccharomyces cerevisiae; Thallophyta
• ISSN: 0022-1287; 1350-0872; 1465-2080
• DOI: 10.1099/00221287-135-6-1453

1 Instituto de Investigaciones Biomédicas del Consejo Superior de Investigaciones Cientificas 2 Departamento de Bioquímica de la Facultad de Medicina de la Universidad Autónoma de Madrid 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. Present address: European Molecular Biology Laboratory, Postfach 102209, 6900 Heidelberg, FRG. Present address: Department of Biology, B-022, University of California, San Diego, La Jolla, CA 92093, USA.