Yeast Hog1 proteins are sequestered in stress granules during high-temperature stress
Yeast Hog1 proteins are sequestered in stress granules during high-temperature stress
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DOI：
10.1242/jcs.209114
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发表时间：
2018-01
影响因子：
4
通讯作者：
Kosuke Shiraishi;T. Hioki;Akari Habata;H. Yurimoto;Y. Sakai
中科院分区：
文献类型：
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作者：
Kosuke Shiraishi;T. Hioki;Akari Habata;H. Yurimoto;Y. Sakai
摘要酵母高渗甘油（HOG）途径在应激反应中起着重要作用。它被各种应激激活，包括高渗应激、氧化应激、高温应激和暴露于亚砷酸盐。Hog 1是该途径的关键MAP激酶，在高渗透浓度（即高渗透压）下定位于细胞核;但除此之外，对其细胞内动力学和调控知之甚少。通过使用甲基营养型酵母博伊丁假丝酵母，我们发现CbHog 1-Venus在高温胁迫后以可逆的方式形成细胞内的点结构。显微镜下观察发现，CbHog 1-mCherry与胁迫颗粒的标记蛋白CbPab 1-Venus共定位。巴斯德毕赤酵母和粟酒裂殖酵母中的Hog 1同源物在高温胁迫下也表现出类似的斑点形成，而酿酒酵母Hog 1（ScHog 1）-GFP则没有。对C. boidinii揭示了N端区域的β折叠结构对于其定位于应力颗粒是必要的和充分的。生理学研究表明，在高温胁迫下，胁迫颗粒中的激活Hog 1蛋白的螯合是Hog 1活性下调的原因。这篇文章有一个相关的第一人称采访的论文的第一作者。总结：在高温胁迫下，酵母MAP激酶Hog 1通过其N端β折叠结构被隔离到胁迫颗粒中，从而下调Hog 1的活性，避免细胞死亡。
ABSTRACT The yeast high-osmolarity glycerol (HOG) pathway plays a central role in stress responses. It is activated by various stresses, including hyperosmotic stress, oxidative stress, high-temperature stress and exposure to arsenite. Hog1, the crucial MAP kinase of the pathway, localizes to the nucleus in response to high osmotic concentrations, i.e. high osmolarity; but, otherwise, little is known about its intracellular dynamics and regulation. By using the methylotrophic yeast Candida boidinii, we found that CbHog1-Venus formed intracellular dot structures after high-temperature stress in a reversible manner. Microscopic observation revealed that CbHog1-mCherry colocalized with CbPab1-Venus, a marker protein of stress granules. Hog1 homologs in Pichia pastoris and Schizosaccharomyces pombe also exhibited similar dot formation under high-temperature stress, whereas Saccharomyces cerevisiae Hog1 (ScHog1)-GFP did not. Analysis of CbHog1-Venus in C. boidinii revealed that a β-sheet structure in the N-terminal region was necessary and sufficient for its localization to stress granules. Physiological studies revealed that sequestration of activated Hog1 proteins in stress granules was responsible for downregulation of Hog1 activity under high-temperature stress. This article has an associated First Person interview with the first author of the paper. Summary: Under high-temperature stress, the yeast MAP kinase Hog1 is sequestered into stress granules through its N-terminal β-sheet structure, which downregulates Hog1 activity and circumvents cell death.