Polarized localization of yeast Pbs2 depends on osmostress, the membrane protein Sho1 and Cdc42
Polarized localization of yeast Pbs2 depends on osmostress, the membrane protein Sho1 and Cdc42
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DOI：
10.1038/35023568
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发表时间：
2000-09
影响因子：
21.3
通讯作者：
V. Reiser;Suhal M. Salah;G. Ammerer
中科院分区：
文献类型：
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作者：
V. Reiser;Suhal M. Salah;G. Ammerer
在酿酒酵母细胞中，高的外部渗透压导致p38相关的丝裂原活化蛋白（MAP）激酶通过Pbs 2的激活。用绿色荧光蛋白标记的Pbs 2（Pbs 2-GFP）在暴露于胁迫之前和之后均匀地分布在细胞质中，但被排除在细胞核之外。在这里，我们表明，一个催化非活性形式的PbS 2达到一个高度极化的本地化过程中的应力。这种现象取决于传感器Sho 1和功能Cdc 42 GTdR。Cdc 42，而不是肌动蛋白细胞骨架，影响Sho 1依赖的激活MAP激酶。Sho 1本身积累在极地生长的网站，但独立的应力条件和Cdc 42。这些观察使我们能够定义在压力信号传播过程中发生的事件的顺序。
In Saccharomyces cerevisiae cells, high external osmolarity leads to the activation of a p38-related mitogen-activated protein (MAP) kinase though Pbs2. Pbs2 tagged with green fluorescent protein (Pbs2–GFP) is evenly distributed in the cytoplasm but excluded from the nucleus before and after exposure to stress. Here we show that a catalytically inactive form of Pbs2 attains a highly polarised localization during osmostress. This phenomenon depends of the osmosensor Sho1 and on a functional Cdc42 GTPase. Cdc42, but not the actin cytoskeleton, influences Sho1-dependent activation of the MAP kinase. Sho1 itself accumulates at sites of polar growth, but independently of stress conditions and Cdc42. These observations allow us to define the sequence of events that occurs during propogation of osmostress signals.