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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Roles of two protein phosphatases, Reg1-Glc7 and Sit4, and glycogen synthesis in regulation of SNF1 protein kinase
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Roles of two protein phosphatases, Reg1-Glc7 and Sit4, and glycogen synthesis in regulation of SNF1 protein kinase

机译：两种蛋白质磷酸酶Reg1-Glc7和Sit4以及糖原合成在SNF1蛋白激酶调节中的作用

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摘要

The SNF1 protein kinase of Saccharomyces cerevisiae is a member of the SNF1/AMP-activated protein kinase family, which is essential for metabolic control, energy homeostasis, and stress responses in eukaryotes. SNF1 is activated in response to glucose limitation by phosphorylation of Thr210 on the activation loop of the catalytic subunit Snf1. The SNF1 p-subunit contains a glycogen-binding domain that has been implicated in glucose inhibition of Snf1 Thr210 phosphorylation. To assess the role of glycogen, we examined Snf1 phosphorylation in strains with altered glycogen metabolism. A reg1△ mutant, lacking Reg1-Glc7 protein phosphatase 1, exhibits elevated glycogen accumulation and phosphorylation of Snf1 during growth on high levels of glucose. Unexpectedly, mutations that abolished glycogen synthesis also restored Thr210 dephosphoryla-tion in glucose-grown regiA cells, indicating that elevated glycogen synthesis contributes to activation of SNF1 and that another phosphatase acts on Snf1. We present evidence that Sit4, a type 2A-like protein phosphatase, contributes to dephosphorylation of Snf1 Thr210. Finally, evidence that the effects of glycogen are not mediated by binding to the p-subunit raises the possibility that elevated glycogen synthesis alters glucose metabolism and thereby reduces glucose signaling to the SNF1 pathway.
机译：酿酒酵母的SNF1蛋白激酶是SNF1 / AMP激活的蛋白激酶家族的成员，该家族对于真核生物的代谢控制，能量稳态和应激反应至关重要。响应葡萄糖限制，通过催化亚基Snf1激活环上的Thr210磷酸化来激活SNF1。 SNF1 p亚基包含一个糖原结合域，已与葡萄糖抑制Snf1 Thr210磷酸化有关。为了评估糖原的作用，我们检查了糖原代谢改变的菌株中的Snf1磷酸化。缺少Reg1-Glc7蛋白磷酸酶1的reg1△突变体在高水平的葡萄糖生长期间表现出升高的糖原积累和Snf1的磷酸化。出乎意料的是，废除糖原合成的突变也恢复了葡萄糖生长的regiA细胞中的Thr210去磷酸化，表明糖原合成的升高有助于SNF1的激活，而另一种磷酸酶作用于Snf1。我们目前的证据，Sit4，一种2A型蛋白磷酸酶，有助于Snf1 Thr210的去磷酸化。最后，糖原作用不受与p-亚基结合介导的证据增加了糖原合成增加改变葡萄糖代谢从而减少葡萄糖向SNF1信号通路的可能性。

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  • 作者

    Amparo Ruiz; Xinjing Xu; Marian Carlson;

  • 作者单位

    Department of Genetics and Development and Department of Microbiology and Immunology, Columbia University, New York, NY 10032;

    Department of Genetics and Development and Department of Microbiology and Immunology, Columbia University, New York, NY 10032;

    Department of Genetics and Development and Department of Microbiology and Immunology, Columbia University, New York, NY 10032;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    glucose regulation; signal transduction; yeast;

    机译：葡萄糖调节信号转导酵母;

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