The mitogen-activated protein kinase Slt2 modulates arsenite transport through the aquaglyceroporin Fps1
The mitogen-activated protein kinase Slt2 modulates arsenite transport through the aquaglyceroporin Fps1
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DOI：
10.1002/1873-3468.12390
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发表时间：
2016-10-01
期刊：
影响因子：
3.5
通讯作者：
Hohmann, Stefan
中科院分区：
文献类型：
--
作者：
Ahmadpour, Doryaneh;Maciaszczyk-Dziubinska, Ewa;Hohmann, Stefan
亚砷酸盐广泛存在于自然界中，因此，细胞已经进化出阻止亚砷酸盐流入并促进流出的机制。在酵母（酿酒酵母）中，水甘油孔蛋白Fps1介导亚砷酸盐流入和流出。丝裂原活化蛋白激酶（MAPK）Hog1以前已被证明限制亚砷酸盐流入通过Fps1。在这项研究中，我们表明，另一个MAPK，Slt2，是短暂的磷酸化，在响应亚砷酸盐流入。我们的研究结果表明，Slt2的蛋白激酶活性是其在砷耐受中的作用所必需的。Hog1通过在Fps1的N端结构域磷酸化T231来阻止亚砷酸盐流入，而Slt2通过在C端磷酸化S537来促进亚砷酸盐流出。我们的数据表明，Slt2与Fps1物理相互作用，这种相互作用依赖于S537的磷酸化。我们推测Hog1和Slt2可能相互影响Fps1的结合，从而控制通道的打开和关闭。
Arsenite is widely present in nature; therefore, cells have evolved mechanisms to prevent arsenite influx and promote efflux. In yeast (Saccharomyces cerevisiae), the aquaglyceroporin Fps1 mediates arsenite influx and efflux. The mitogen-activated protein kinase (MAPK) Hog1 has previously been shown to restrict arsenite influx through Fps1. In this study, we show that another MAPK, Slt2, is transiently phosphorylated in response to arsenite influx. Our findings indicate that the protein kinase activity of Slt2 is required for its role in arsenite tolerance. While Hog1 prevents arsenite influx via phosphorylation of T231 at the N-terminal domain of Fps1, Slt2 promotes arsenite efflux through phosphorylation of S537 at the C terminus. Our data suggest that Slt2 physically interacts with Fps1 and that this interaction depends on phosphorylation of S537. We hypothesize that Hog1 and Slt2 may affect each other's binding to Fps1, thereby controlling the opening and closing of the channel.