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FERONIA phosphorylates E3 ubiquitin ligase ATL6 to modulate the stability of 14-3-3 proteins in response to the carbon/nitrogen ratio

文献类型： 外文期刊

作者： Xu, Guoyun 1 ; Chen, Weijun 2 ; Song, Limei 2 ; Chen, Qiansi 1 ; Zhang, Hui 1 ; Liao, Hongdong 2 ; Zhao, Guoqiang 5 ; Lin 1 ;

作者机构： 1.China Natl Tobacco Corp, Zhengzhou Tobacco Res Inst, Zhengzhou 450001, Henan, Peoples R China

2.Hunan Univ, State Key Lab Chemo Biosensing & Chemometr, Coll Biol, Changsha 410082, Hunan, Peoples R China

3.Hunan Univ, Hunan Key Lab Plant Funct Genom & Dev Regulat, Changsha 410082, Hunan, Peoples R China

4.Zhejiang Univ, Inst Biotechnol, State Key Lab Rice Biol, Hangzhou 310058, Zhejiang, Peoples R China

5.Zhengzhou Univ, Sch Basic Med Sci, Zhengzhou 450001, Henan, Peoples R China

6.Hunan Hybrid Rice Res Ctr, State Key Lab Hybrid Rice, Changsha 410125, Hunan, Peoples R China

关键词： Arabidopsis thaliana; ATL6; carbon; nitrogen response; E3 ubiquitin ligase; FERONIA; phosphorylation; RALF1; 14-3-3 protein

期刊名称：JOURNAL OF EXPERIMENTAL BOTANY （ 影响因子：6.992； 五年影响因子：7.86 ）

ISSN： 0022-0957

年卷期： 2019 年 70 卷 21 期

页码：

收录情况： SCI

摘要： The ratio between carbon (C) and nitrogen (N) utilization must be precisely coordinated to enable plant growth. Although numerous physiological studies have examined carbon/nitrogen (C/N) ratios, the mechanisms of sensing the C/N balance and C/N signaling remain elusive. Here, we report that a mutation of FERONIA (FER), a receptor kinase that plays versatile roles in plant cell growth and stress responses, caused hypersensitivity to a high C/N ratio in Arabidopsis. In contrast, FER-overexpressing plants displayed more resistant phenotypes. FER can interact with and phosphorylate ATL6, an E3 ubiquitin ligase that has been shown to regulate plant C/N responses. FER-mediated ATL6 phosphorylation enhanced the interaction between ATL6 and its previously identified target 14-3-3 proteins, thus decreasing 14-3-3 protein levels, leading to an increased insensitivity to high C/N ratios. Further analyses showed that the rapid alkalinization factor peptide (RALF1), which is a ligand of FER, also influenced the stability of 14-3-3 proteins via a FER-ATL6-mediated pathway. These findings reveal a novel regulatory mechanism that links the RALF1/FER-ATL6 pathway to whole-plant C/N responses and growth.

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