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

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

作者机构：State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresourcesCollege of Life Science and TechnologyGuangxi Key Laboratory for Sugarcane BiologyGuangxi UniversityNanning 530004P.R.China State Key Laboratory of Chemo/Biosensing and ChemometricsCollege of BiologyHunan Key Laboratory of Plant Functional Genomics and Developmental RegulationHunan UniversityChangsha 410082P.R.China State Key Laboratory of Hybrid RiceHunan Hybrid Rice Research CenterChangsha 410125P.R.China Shanghai Synchrotron Radiation FacilityShanghai Advanced Research InstituteChinese Academy of SciencesShanghaiP.R.China 

出 版 物：《Plant Communications》 (植物通讯（英文）)

年 卷 期：2023年第4卷第4期

页      面：132-145页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学] 

基　　金：supported by grants from the National Natural Science Foundation of China(32160064,31871396,31571444,and 32000916) the State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources(SKLCUSA-a201806) the China Postdoctoral Science Foundation(2019M662764) the Hunan Provincial Natural Science Foundation of China(2021JJ40050) the Guangxi Natural Science Foundation(2020GXNSFFA297007) the Guangxi Key Laboratory for Sugarcane Biology(GXKLSCB-20190304) 

主　　题：FERONIA active conformation kinase activity autophosphorylation activation 

摘      要：Accumulating evidence indicates that early and essential events for receptor-like kinase(RLK)function involve both autophosphorylation and substrate ***,the structural and biochemical basis for these events is largely ***,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 Mg^(2+) in the unphosphorylated *** FER-KD was found to adopt an unexpected active conformation in its crystal ***,unphosphorylated FER-KD mutants with reduced(S525A)or no catalytic activity(K565R)also adopt similar active *** studies revealed that FER-KD is a dual-specificity kinase,and its autophosphorylation is accomplished via an intermolecular *** investigations confirmed that initiating substrate phosphorylation requires autophosphorylation of the activation segment on T696,S701,and *** 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.