Global mapping of protein phosphorylation events identifies Ste20, Sch9 and the cell-cycle regulatory kinases Cdc28/Pho85 as mediators of fatty acid starvation responses in Saccharomyces cerevisiae
Global mapping of protein phosphorylation events identifies Ste20, Sch9 and the cell-cycle regulatory kinases Cdc28/Pho85 as mediators of fatty acid starvation responses in Saccharomyces cerevisiae
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DOI：
10.1039/c2mb05356j
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发表时间：
2012-01-01
影响因子：
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通讯作者：
Faergeman, Nils J.
中科院分区：
文献类型：
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作者：
Pultz, Dennis;Bennetzen, Martin V.;Faergeman, Nils J.
脂肪酸的合成、降解和代谢是严格协调的，以满足细胞和生物体的营养和能量需求。在缺乏外源脂肪酸的情况下，酵母Saccharomyces cerevisiae的增殖和生长依赖于脂肪酸的内源性合成，其由脂肪酸合成酶催化。在本研究中，我们已经使用定量蛋白质组学研究细胞反应抑制脂肪酸合成的酿酒酵母。我们已经确定了大约2000个磷酸化位点，其中400多个已被确定为在时间上受到调节，以响应浅蓝菌素对脂肪酸合成的抑制。通过对这些磷酸化事件的生物信息学分析，我们已经确定了细胞周期激酶Cdc28和Pho85，PAK激酶Ste20以及蛋白激酶Sch9作为细胞对脂肪酸合成抑制反应的中心介质。
Synthesis, degradation, and metabolism of fatty acids are strictly coordinated to meet the nutritional and energetic needs of cells and organisms. In the absence of exogenous fatty acids, proliferation and growth of the yeast Saccharomyces cerevisiae depends on endogenous synthesis of fatty acids, which is catalysed by fatty acid synthase. In the present study, we have used quantitative proteomics to examine the cellular response to inhibition of fatty acid synthesis in Saccharomyces cerevisiae. We have identified approximately 2000 phosphorylation sites of which more than 400 have been identified as being regulated in a temporal manner in response to inhibition of fatty acid synthesis by cerulenin. By bioinformatic analysis of these phosphorylation events, we have identified the cell cycle kinases Cdc28 and Pho85, the PAK kinase Ste20 as well as the protein kinase Sch9 as central mediators of the cellular response to inhibition of fatty acid synthesis.