Structural analysis of receptor-like kinase SOBIR1 reveals mechanisms that regulate its phosphorylation-dependent activation

作     者：Xue Wei Yulu Wang Su Zhang Tianyi Gu Gabryel Steinmetz Haiyan Yu Guoguang Guo Xin Liu Shilong Fan Fengzhong Wang Yangnan Gu Fengjiao Xin 

作者机构：Laboratory of Biomanufacturing and Food EngineeringInstitute of Food Science and TechnologyChinese Academy of Agricultural SciencesBeijing 100193China Beijing Advanced Innovation Center for Tree Breeding by Molecular DesignBeijing Forestry UniversityBeijing 100083China Department of Plant and Microbial BiologyUniversity of CaliforniaBerkeleyCA 94720USA Innovative Genomics InstituteUniversity of CaliforniaBerkeleyCA 94720USA Key Laboratory of Ministry of Education for Protein ScienceSchool of Life SciencesTsinghua UniversityBeijing 100084China Hefei National Laboratory for Physical Sciences at the Microscale and School of Life SciencesUniversity of Science and Technology of ChinaHefeiAnhui 230026China The Center of Protein ScienceTsinghua UniversityBeijing 100084China 

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

年 卷 期：2022年第3卷第2期

页      面：34-51页

核心收录：

学科分类：0710[理学-生物学] 09[农学] 0903[农学-农业资源与环境] 

基　　金：This work was supported by the National Natural Science Foundation of China(31571963) 

主　　题：LRR-RLK SOBIR1 crystal structure unusual architecture autophosphorylation stepwise activation 

摘      要：Plant leucine-rich repeat(LRR)receptor-like kinases(RLKs)and LRR receptor-like proteins(RLPs)comprise a large family of cell surface receptors that play critical roles in signal perception and *** LRR-RLKs and LRR-RLPs rely on regulatory LRR-RLKs to initiate downstream signaling *** INSENSITIVE 1-ASSOCIATED KINASE 1/SOMATIC EMBRYOGENESIS RECEPTOR KINASE 3(BAK1/SERK3)and SUPPRESSOR OF BIR1-1(SOBIR1)are important and extensively studied regulatory LRR-RLKs with distinct *** the regulatory mechanism of BAK1 activation has been studied in detail,the activation mechanism of SOBIR1 remains poorly ***,the crystal structures of the catalytically inactive kinase domain of SOBIR1(SOBIR1-KD)from Arabidopsis thaliana were determined in complexes with AMP-PNP and Mg^(2+).The results show that SOBIR1-KD contains a uniquely long β3-αC loop and adopts an Src-like inactive conformation with an unusual architecture at the activation segment,which comprises three *** studies revealed that SOBIR1 is transphosphorylated by BAK1 following its autophosphorylation via an intermolecular mechanism,and the phosphorylation of Thr529 in the activation segment and the β3-αC loop are critical for SOBIR1 *** functional analysis confirmed the importance of Thr529 and the β3-αC loop for the SOBIR1-induced cell death response in Nicotiana *** together,these findings provide a structural basis for the regulatory mechanism of SOBIR1 and reveal the important elements and phosphorylation events in the special stepwise activation of SOBIR1-KD,the first such processes found in regulatory LRR-RLKs.