Mutual Regulation of Receptor-Like Kinase SIT1 and B 'kappa-PP2A Shapes the Early Response of Rice to Salt Stress
文献类型： 外文期刊
作者： Zhao, Ji-Long 1 ; Zhang, Li-Qing 1 ; Li, Ning 1 ; Xu, Shou-Ling 2 ; Yue, Zhi-Liang 1 ; Zhang, Lu-Lu 1 ; Deng, Zhi-Ping 4 ;
作者机构： 1.Hebei Normal Univ, Hebei Collaborat Innovat Ctr Cell Signaling, Hebei Key Lab Mol & Cellular Biol, Key Lab Mol & Cellular Biol,Minist Educ,Coll Life, Shijiazhuang 050024, Hebei, Peoples R China
2.Carnegie Inst Sci, Dept Plant Biol, Stanford, CA 94305 USA
3.Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA
4.Zhejiang Acad Agr Sci, Inst Virol & Biotechnol, State Key Lab Breeding Base Zhejiang Sustainable, Hangzhou 310021, Zhejiang, Peoples R China
期刊名称：PLANT CELL （ 影响因子：11.277； 五年影响因子：12.061 ）
ISSN： 1040-4651
年卷期： 2019 年 31 卷 9 期
页码：
收录情况： SCI
摘要： The receptor-like kinase SIT1 acts as a sensor in rice (Oryza sativa) roots, relaying salt stress signals via elevated kinase activity to enhance salt sensitivity. Here, we demonstrate that Protein Phosphatase 2A (PP2A) regulatory subunit B'kappa constrains SIT1 activity under salt stress. B'kappa-PP2A deactivates SIT1 directly by dephosphorylating the kinase at Thr515/516, a salt-induced phosphorylation site in the activation loop that is essential for SIT1 activity. B'kappa overexpression suppresses the salt sensitivity of rice plants expressing high levels of SIT1, thereby contributing to salt tolerance. B'kappa functions in a SIT1 kinase-dependent manner. During early salt stress, activated SIT1 phosphorylates B'kappa; this not only enhances its binding with SIT1, it also promotes B'kappa protein accumulation via Ser502 phosphorylation. Consequently, by blocking SIT1 phosphorylation, B'kappa inhibits and fine-tunes SIT1 activity to balance plant growth and stress adaptation.
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