Glucose regulates protein interactions within the yeast SNF1 protein kinase complex
Glucose regulates protein interactions within the yeast SNF1 protein kinase complex
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DOI：
10.1101/gad.10.24.3105
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发表时间：
1996-12-15
影响因子：
10.5
通讯作者：
Carlson, M
中科院分区：
文献类型：
--
作者：
Jiang, R;Carlson, M
SNF1蛋白激酶在真核生物中广泛保守，并与茶叶环境和营养胁迫的反应有关。在酵母中，SNF1激酶在葡萄糖饥饿反应中起着重要作用。SNF1与其活化亚基SNF4和其他蛋白质形成复合物。使用双杂交系统，我们表明，SNF1和SNF4之间的相互作用是强烈的葡萄糖信号调节。此外，这种相互作用受到调节因子（包括蛋白磷酸酶1）突变的适当影响。我们发现，SNF4结合SNF1的调节结构域在低葡萄糖，而在高葡萄糖的调节结构域结合SNF1本身的激酶结构域。遗传分析进一步表明，SNF1调节结构域自抑制激酶活性，在低葡萄糖SNF4拮抗这种抑制。最后，这些相互作用已被保存从酵母到植物，表明SNF1激酶复合物的同源物通过类似的机制响应调节信号。
The SNF1 protein kinase is broadly conserved in eukaryotes and has been implicated in responses tea environmental and nutritional stress. In yeast, the SNF1 kinase has a central role in the response to glucose starvation. SNF1 is associated with its activating subunit, SNF4, and other proteins in complexes. Using the two-hybrid system, we show that interaction between SNF1 and SNF4 is strongly regulated by the glucose signal. Moreover, this interaction is appropriately affected by mutations in regulators, including protein phosphatase 1. We show that SNF4 binds to the SNF1 regulatory domain in low glucose, whereas in high glucose the regulatory domain binds to the kinase domain of SNF1 itself. Genetic analysis further suggests that the SNF1 regulatory domain autoinhibits the kinase activity and that in low glucose SNF4 antagonizes this inhibition. Finally, these interactions have been conserved from yeast to plants, indicating that homologs of the SNF1 kinase complex respond to regulatory signals by analogous mechanisms.