The protein phosphatase 2C clade A TaPP2CA interact with calcium-dependent protein kinases, TaCDPK5/TaCDPK9-1, that phosphorylate TabZIP60 transcription factor from wheat (Triticum aestivum L.)

文献类型： 外文期刊

第一作者： Zhang, Lina

作者： Zhang, Lina;Wang, Liting;Chen, Xue;Zhao, Lijuan;Liu, Xingyan;Wu, Guofan;Wang, Yinghong;Xia, Chuan;Zhang, Lichao;Kong, Xiuying

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关键词： Wheat; TaCDPK5/TaCDPK9-1; TabZIP60 TF; Phosphorylation; TaPP2CA116/ TaPP2CA 121

期刊名称：PLANT SCIENCE （ 影响因子：5.363； 五年影响因子：5.454 ）

ISSN： 0168-9452

年卷期： 2022 年 321 卷

页码：

收录情况： SCI

摘要： Previously we have found that TabZIP60 from the ABF/AREB (ABRE-binding factor/ABA-responsive element-binding protein) subfamily of bZIP transcription factor (TF) was involved in salt stress response. However, the regulatory mechanism of TabZIP60 is unknown. In the present study, we identified two calcium-dependent protein kinase (CDPK) genes, TaCDPK5/TaCDPK9-1, which were clustered into group I and were induced by salt, abscisic acid (ABA), and polyethylene glycol (PEG) treatments. RT-qPCR results showed that the expression level of salt-induced TabZIP60 was drastically inhibited by Ca2+ channel blocker LaCl3. TaCDPK5/TaCDPK9-1 were involved in interaction with TabZIP60 protein in vivo and in vitro. And TaCDPK5/TaCDPK9-1 could autophosphorylate and phosphorylate TabZIP60 protein in a Ca2+-dependent way. Mutational analysis indicated that Serine-110 of TabZIP60 was essential for TaCDPK5/TaCDPK9-1-TabZIP60 interaction and was the phosphorylation site of TaCDPK5/TaCDPK9-1 kinases. Yeast two-hybrid assay results showed the interactions between TaCDPK5/TaCDPK9-1 and wheat protein phosphatase 2 C clade A TaPP2CA116/ TaPP2CA121 separately. These findings demonstrate that the phosphorylation status of TabZIP60 controlled by TaPP2CA116/ TaPP2CA121 and TaCDPK5/TaCDPK9-1 might play a crucial role in wheat during salt stress.

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