Structural and biochemical basis of Arabidopsis FERONIA receptor kinase-mediated early signaling initiation

文献类型： 外文期刊

第一作者： Kong, Yanqiong

作者： Kong, Yanqiong;Ming, Zhenhua;Chen, Jia;Jiang, Lingli;Chen, Hong;Shen, Yanan;Yan, Yujie;Zheng, Heping;Yu, Feng;Wang, Lifeng;Yu, Feng;Zhou, Huan

作者机构：

关键词： FERONIA; active conformation; kinase activity; autophosphorylation; activation

期刊名称：PLANT COMMUNICATIONS （ 影响因子：10.5； 五年影响因子：10.5 ）

ISSN： 2590-3462

年卷期： 2023 年 4 卷 4 期

页码：

收录情况： SCI

摘要： Accumulating evidence indicates that early and essential events for receptor-like kinase (RLK) function involve both autophosphorylation and substrate phosphorylation. However, the structural and biochemical basis for these events is largely unclear. Here, we used RLK FERONIA (FER) as a model and crystallized its core kinase domain (FER-KD) and two FER-KD mutants (K565R, S525A) in complexes with ATP/ADP and Mg2+ in the unphosphorylated state. Unphosphorylated FER-KD was found to adopt an unexpected active conformation in its crystal structure. Moreover, unphosphorylated FER-KD mutants with reduced (S525A) or no catalytic activity (K565R) also adopt similar active conformations. Biochemical studies revealed that FER-KD is a dual-specificity kinase, and its autophosphorylation is accomplished via an intermolecular mechanism. Further investigations confirmed that initiating substrate phosphorylation requires autophos-phorylation of the activation segment on T696, S701, and Y704. This study reveals the structural and biochemical basis for the activation and regulatory mechanism of FER, providing a paradigm for the early steps in RLK signaling initiation.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序