The serine/threonine kinase Cmk2 is required for oxidative stress response in fission yeast
The serine/threonine kinase Cmk2 is required for oxidative stress response in fission yeast
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DOI：
10.1074/jbc.m200104200
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发表时间：
2002-05-17
影响因子：
4.8
通讯作者：
Aligue, R
中科院分区：
文献类型：
--
作者：
Sánchez-Piris, M;Posas, F;Aligue, R
Cmk 2是一种与哺乳动物钙调蛋白激酶同源的裂殖酵母Ser/Thr蛋白激酶，是氧化应激反应所必需的。缺乏cmk 2基因的细胞对氧化应激条件特别敏感。在应激时，Cmk 2在体内被磷酸化，并且这种磷酸化依赖于应激激活的MAPK Sty 1/Spc 1。共沉淀分析表明，Cmk 2结合Sty 1。此外，在体内或体外激活的Sty 1能够磷酸化Cmk 2，磷酸化发生在C-末端调节结构域的Thr-411。Wis 1 MAPK激酶过表达引起的细胞致死性被cmk 2缺失或Cmk 2的Thr-411突变所消除。两者合计，我们的数据表明，Cmk 2的行为下游的Sty 1和氧化应激反应是一个必不可少的激酶。
Cmk2, a fission yeast Ser/Thr protein kinase homologous to mammalian calmodulin kinases, is essential for oxidative stress response. Cells lacking cmk2 gene were specifically sensitive to oxidative stress conditions. Upon stress, Cmk2 was phosphorylated in vivo, and this phosphorylation was dependent on the stress-activated MAPK Sty1/Spc1. Co-precipitation assays demonstrated that Cmk2 binds Sty1. Furthermore, in vivo or in vitro activated Sty1 was able to phosphorylate Cmk2, and the phosphorylation occurred at the C-terminal regulatory domain at Thr-411. Cell lethality caused by overexpression of Wis1 MAPK kinase was abolished by deletion of cmk2 or by mutation of Thr-411 of Cmk2. Taken together, our data suggest that Cmk2 acts downstream of Sty1 and is an essential kinase for oxidative stress responses.