Structural and biochemical basis of Arabidopsis FERONIA receptor kinase-mediated early signaling initiation
文献类型： 外文期刊
作者： Kong, Yanqiong 1 ; Chen, Jia 2 ; Jiang, Lingli 2 ; Chen, Hong 2 ; Shen, Yanan 2 ; Wang, Lifeng 3 ; Yan, Yujie 2 ; Zhou, Huan 4 ; Zheng, Heping 2 ; Yu, Feng 2 ; Ming, Zhenhua 1 ;
作者机构： 1.Guangxi Univ, State Key Lab Conservat & Utilizat Subtrop Agrobio, Coll Life Sci & Technol, Guangxi Key Lab Sugarcane Biol, Nanning 530004, Peoples R China
2.Hunan Univ, Coll Biol, State Key Lab Chemo Biosensing & Chemometr, Hunan Key Lab Plant Funct Genom & Dev Regulat, Changsha 410082, Peoples R China
3.Hunan Hybrid Rice Res Ctr, State Key Lab Hybrid Rice, Changsha 410125, Peoples R China
4.Chinese Acad Sci, Shanghai Adv Res Inst, Shanghai Synchrotron Radiat Facil, Shanghai, Peoples R China
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.
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