Mazón M J, Behrens M M, Portillo F, Piñón R
Instituto de Investigaciones del Consejo Superior, Madrid
J Gen Microbiol. 1989 Jun;135(6):1453-60. doi: 10.1099/00221287-135-6-1453.
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.
酿酒酵母的质膜ATP酶是一种质子泵，其活性对于细胞增殖至关重要，并受到营养信号的调节。先前的研究发现，葡萄糖诱导的H⁺-ATP酶激活需要CDC25基因产物，这表明H⁺-ATP酶活性受cAMP调节。对RAS蛋白、腺苷酸环化酶或cAMP依赖性蛋白激酶活性受影响的突变体中饥饿诱导的H⁺-ATP酶失活和葡萄糖诱导的激活进行分析，结果表明H⁺-ATP酶活性的营养调节并不直接依赖于这些因素中的任何一个。我们得出结论，腺苷酸环化酶并不介导所有的营养反应。这也表明，葡萄糖诱导的H⁺-ATP酶激活对CDC25的特定需求确定了CDC25基因产物的一个新功能，该功能似乎独立于CDC25介导的RAS/腺苷酸环化酶/cAMP途径的调节。
