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

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

doi:10.1016/j.xplc.2023.100559

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

Plant Commun. 2023 Jul 10;4(4):100559. doi: 10.1016/j.xplc.2023.100559. Epub 2023 Feb 11.

Authors

Yanqiong Kong¹, Jia Chen², Lingli Jiang², Hong Chen², Yanan Shen², Lifeng Wang³, Yujie Yan², Huan Zhou⁴, Heping Zheng², Feng Yu⁵, Zhenhua Ming⁶

Affiliations

¹ State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Life Science and Technology, Guangxi Key Laboratory for Sugarcane Biology, Guangxi University, Nanning 530004, P.R. China.
² State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Biology, Hunan Key Laboratory of Plant Functional Genomics and Developmental Regulation, Hunan University, Changsha 410082, P.R. China.
³ State Key Laboratory of Hybrid Rice, Hunan Hybrid Rice Research Center, Changsha 410125, P.R. China.
⁴ Shanghai Synchrotron Radiation Facility, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai, P.R. China.
⁵ State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Biology, Hunan Key Laboratory of Plant Functional Genomics and Developmental Regulation, Hunan University, Changsha 410082, P.R. China; State Key Laboratory of Hybrid Rice, Hunan Hybrid Rice Research Center, Changsha 410125, P.R. China. Electronic address: feng_yu@hnu.edu.cn.
⁶ State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Life Science and Technology, Guangxi Key Laboratory for Sugarcane Biology, Guangxi University, Nanning 530004, P.R. China. Electronic address: zhming@gxu.edu.cn.

Abstract

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 autophosphorylation 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.

Keywords: FERONIA; activation; active conformation; autophosphorylation; kinase activity.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Arabidopsis Proteins* / metabolism
Arabidopsis* / metabolism
Phosphorylation
Signal Transduction / physiology

Substances

Arabidopsis Proteins