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

引用

Plant Communications 2022年第2期3卷 34-51页

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 Laboratory of Biomanufacturing and Food Engineering Institute of Food Science and TechnologyChinese Academy of Agricultural SciencesBeijing 100193China Beijing Advanced Innovation Center for Tree Breeding by Molecular Design Beijing Forestry UniversityBeijing 100083China Department of Plant and Microbial Biology University of CaliforniaBerkeleyCA 94720USA Innovative Genomics Institute University of CaliforniaBerkeleyCA 94720USA Key Laboratory of Ministry of Education for Protein Science School of Life SciencesTsinghua UniversityBeijing 100084China Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences University of Science and Technology of ChinaHefeiAnhui 230026China The Center of Protein Science Tsinghua UniversityBeijing 100084China

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.

关键词： LRR-RLK SOBIR1 crystal structure unusual architecture autophosphorylation stepwise activation

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