Subcellular localization of VIP1 is regulated by phosphorylation and 14-3-3 proteins
Subcellular localization of VIP1 is regulated by phosphorylation and 14-3-3 proteins
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DOI：
10.1002/1873-3468.12686
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发表时间：
2017-07-01
期刊：
影响因子：
3.5
通讯作者：
Ito, Takeshi
中科院分区：
文献类型：
--
作者：
Takeo, Koichi;Ito, Takeshi
拟南芥碱性亮氨酸拉链转录因子VIRE2相互作用蛋白1(VIP1)在细胞受到机械胁迫或低渗透胁迫时，将其定位从胞浆改变到细胞核，尽管这种变化的机制尚不清楚。在这项研究中，我们发现VIP1亚细胞定位的改变与机械/低渗透应激诱导的VIP1磷酸化状态的改变是同步的。VIP1在HXRXXS基序中有三个可磷酸化的丝氨酸残基，是14-3-3结合的靶标。这些残基的突变导致14-3-3结合的缺失，并阻止VIP1的胞内定位。这些结果表明，机械应激或低渗应激引起的VIP1去磷酸化通过14-3-3解离诱导核定位。
Arabidopsis basic leucine zipper transcription factor VIRE2-interacting protein 1 (VIP1) changes its localization from the cytosol to the nucleus when cells are subjected to mechanical or hypo-osmotic stress, although the mechanism of this change is not known. In this study, we show that change in VIP1 subcellular localization is synchronized with a change in the VIP1 phosphorylation state that is induced by mechanical/hypo-osmotic stress. VIP1 has three phosphorylatable serine residues in HXRXXS motifs, which are 14-3-3-binding targets. Mutations of these residues results in the lack of 14-3-3 binding and prevents cytosolic localization of VIP1. These results suggest that dephosphorylation of VIP1 resulting from mechanical or hypo-osmotic stress induces nuclear localization via 14-3-3 dissociation.