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Calcium signaling and sugar-induced activation of plasma membrane H+-ATPase in Saccharomyces cerevisiae cells

机译:啤酒酵母细胞中钙信号传导和糖诱导的质膜H + -ATPase活化

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摘要

In this work, we show that glucose-induced activation of plasma membrane H+-ATPase from Saccharomyces cerevisiae is strongly dependent on calcium metabolism and that the glucose sensor Snf3p works in a parallel way with the G protein Gpa2p in the control of the pathway. The role of Snf3p is played by the Snf3p C-terminal tail, since in a strain with the deletion of the SNF3 gene, but also expressing a chimera protein formed by Hxt1p (a glucose transporter) and the Snf3p C-terminal tail, a normal glucose-activation process can be observed. We present evidences indicating that Snf3p would be the sensor for the internal signal (phosphorylated sugars) of this pathway that would connect calcium signaling and activation of the plasma membrane ATPase. We also show that Snf3p could be involved in the control of Pmc1p activity that would regulate the calcium availability in the cytosol. (c) 2006 Elsevier Inc. All rights reserved.
机译:在这项工作中,我们表明葡萄糖诱导的酿酒酵母质膜H + -ATPase的激活强烈依赖于钙代谢,并且葡萄糖传感器Snf3p与G蛋白Gpa2p在该途径的控制中以并行方式起作用。 Snf3p的作用由Snf3p C末端尾巴发挥,因为在缺失SNF3基因的菌株中,它还表达由Hxt1p(葡萄糖转运蛋白)和Snf3p C末端尾巴(正常)形成的嵌合蛋白。可以观察到葡萄糖活化过程。我们提供的证据表明,Snf3p将是该途径的内部信号(磷酸化糖)的传感器,该途径将连接钙信号传导和质膜ATPase激活。我们还表明,Snf3p可能参与Pmc1p活性的控制,该活性将调节细胞溶质中的钙利用率。 (c)2006 Elsevier Inc.保留所有权利。

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