Dissecting yeast Hog1 MAP kinase pathway using a chemical genetic approach
Dissecting yeast Hog1 MAP kinase pathway using a chemical genetic approach
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DOI：
10.1016/j.febslet.2007.02.032
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发表时间：
2007-03-20
期刊：
影响因子：
3.5
通讯作者：
Shah, Kavita
中科院分区：
文献类型：
--
作者：
Kim, Sungjoon;Shah, Kavita
使用化学遗传学方法，我们确定了四种新的Hog1激酶的生理底物（Krs1，Tdh3，Hsp26和Shm2）。这些基板建议合理的机制肌动蛋白重组，细胞周期阻滞和调节蛋白质合成后观察到渗透胁迫。我们进一步表明，人类同源的Shm2（SHMT1）是一种新的生理底物的p38 MAP激酶在体外和体内。在p38介导的磷酸化后观察到其酶活性的下调，揭示了p38 MAP激酶的潜在癌症调节特性。这个屏幕上发现了几个新的HogI底物，提供了新的途径，调查这种激酶的适应性的机制。(c)2007年欧洲生物化学学会联合会。Elsevier B.V.出版，保留所有权利。
Using a chemical genetic approach, we identified four novel physiological substrates of Hog1 kinase (Krs1, Tdh3, Hsp26, and Shm2). These substrates suggest plausible mechanisms for actin reorganization, cell cycle arrest and regulation of protein synthesis observed upon osmotic stress. We further show that the human homolog of Shm2 (SHMT1) is a novel physiological substrate of p38 MAP kinase in vitro and in vivo. Down-regulation of its enzymatic activity was observed following p38-mediated phosphorylation revealing a potential cancer-modulating property of p38 MAP kinase. This screen has uncovered several novel HogI substrates that provide new avenues for investigation into the mechanism of osmoadaptation by this kinase. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.