Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae.
Nutrient sensing and signaling in the yeast Saccharomyces cerevisiae.
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DOI：
10.1111/1574-6976.12065
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发表时间：
2014-03
影响因子：
11.3
通讯作者：
Thevelein JM
中科院分区：
文献类型：
--
作者：
Conrad M;Schothorst J;Kankipati HN;Van Zeebroeck G;Rubio-Texeira M;Thevelein JM
酿酒酵母一直是营养感测和信号传导机制开创性研究的首选生物。许多特定的营养反应已被详细阐明。这导致了重要的新概念和洞察营养控制的细胞调节。主要亮点包括Snf1蛋白激酶在葡萄糖抑制途径中的核心作用，半乳糖诱导，g蛋白偶联受体系统的发现，Ras在葡萄糖诱导的cAMP信号传导中的作用，蛋白质合成起始机制在氮代谢的一般控制中的作用，细胞周期蛋白控制的蛋白激酶Pho85在磷酸盐调节中的作用，氮分解代谢抑制和雷帕霉素途径的氮传感靶点。以及转运蛋白作为营养传感器的发现。此外，许多细胞靶标，如碳水化合物储存、应激耐受性和核糖体基因表达，都是由多种营养物质的存在控制的。蛋白激酶A信号通路在这种一般的营养反应中起主要作用。它导致了营养受体（转运受体）作为营养传感器的发现。目前我们所知的主要不足是快速和稳态营养信号之间的关系，代谢中间体在细胞内营养感知中的作用，以及控制细胞生长的营养传感器的身份。
The yeast Saccharomyces cerevisiae has been a favorite organism for pioneering studies on nutrient-sensing and signaling mechanisms. Many specific nutrient responses have been elucidated in great detail. This has led to important new concepts and insight into nutrient-controlled cellular regulation. Major highlights include the central role of the Snf1 protein kinase in the glucose repression pathway, galactose induction, the discovery of a G-protein-coupled receptor system, and role of Ras in glucose-induced cAMP signaling, the role of the protein synthesis initiation machinery in general control of nitrogen metabolism, the cyclin-controlled protein kinase Pho85 in phosphate regulation, nitrogen catabolite repression and the nitrogen-sensing target of rapamycin pathway, and the discovery of transporter-like proteins acting as nutrient sensors. In addition, a number of cellular targets, like carbohydrate stores, stress tolerance, and ribosomal gene expression, are controlled by the presence of multiple nutrients. The protein kinase A signaling pathway plays a major role in this general nutrient response. It has led to the discovery of nutrient transceptors (transporter receptors) as nutrient sensors. Major shortcomings in our knowledge are the relationship between rapid and steady-state nutrient signaling, the role of metabolic intermediates in intracellular nutrient sensing, and the identity of the nutrient sensors controlling cellular growth.