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Identifi cation and functional analysis of phosphorylation residues of the Arabidopsis BOTRYTIS-INDUCED KINASE1

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Protein & Cell 2013年第10期4卷 771-781页

作者： Jinhua Xu Xiaochao Wei Limin Yan Dan Liu Yuanyuan Ma Yu Guo Chune Peng Honggang Zhou Cheng Yang Zhiyong Lou Wenqing Shui College of Life Sciences and Tianjin State Laboratory of Protein Science Nankai UniversityTianjin 300071China High-throughput Molecular Drug Discovery Center Tianjin Joint Academy of Biotechnology and MedicineTianjin 300457China Laboratory of Structural Biology and MOE Laboratory of Protein Science School of Medicine and Life SciencesTsinghua UniversityBeijing 100084China College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology Nankai UniversityTianjin 300071China

Arabidopsis BOTRYTIS-INDUCED KINASE1(bik1)is a receptor-like cytoplasmic kinase acting early in multiple signaling pathways important for plant growth and innate *** is known to form a signaling complex with a cell-surface receptor FLS2 and a co-receptor kinase BAK1 to transduce signals upon perception of pathogen-asso-ciated molecular patterns(PAMPs).Although site-specifi c phosphorylation is speculated to mediate the activation and function of bik1,few studies have been devoted to complete profiling of bik1 phosphorylation ***,we identified nineteen in vitro autophosphoryla-tion sites of bik1 including three phosphotyrosine sites,thereby proving bik1 is a dual-specifi city kinase for the fi rst *** kinase activity of bik1 substitution mutants were explicitly assessed using quantitative mass spec-trometry(MS).Thr-237,Thr-242 and Tyr-250 were found to most signifi cantly affect bik1 activity in autophosphoryla-tion and phosphorylation of BAK1 in vitro.A structural model of bik1 was built to further illustrate the molecular functions of specifi c phosphorylation *** also mapped new sites of FLS2 phosphorylation by bik1,which are different from those by *** in vitro results could provide new hypotheses for more in-depth in vivo studies leading to deeper understanding of how phosphorylation contributes to bik1 activation and medi-ates downstream signaling specifi city.

关键词： phosphorylation bik1 receptor-like cytop-lasmic kinase quantitative mass spectrometry

A Xanthomonas oryzae pv. oryzae effector, Xop R, associates with receptor-like cytoplasmic kinases and suppresses PAMP-triggered stomatal closure

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Science China(Life Sciences) 2016年第9期59卷 897-905页

作者： Shuangfeng Wang Jianhang Sun Fenggui Fan Zhaoyun Tan Yanmin Zou Dongping Lu State Key Laboratory of Plant Genomics Center for Agricultural Research Resources Institute of Genetics and Developmental Biology Chinese Academy of Sciences Shijiazhuang Hebei 050021 China University of Chinese Academy of Sciences Beijing 100049 China

Receptor-like kinases(RLKs) play important roles in plant immunity signaling; thus, many are hijacked by pathogen effectors to promote successful pathogenesis. Xanthomonas oryzae pv. oryzae(Xoo) is the causal agent of rice leaf blight disease. The strain PXO99 A has 18 non-TAL(transcription activation-like) effectors; however, their mechanisms of action and host target proteins remain largely unknown. Although the effector XopR from the Xoo strain MAFF311018 was shown to suppress PAMP-triggered immune responses in Arabidopsis, its target has not yet been identified. Here, we show that PXO99 A XopR interacts with bik1 at the plasma membrane. bik1 is a receptor-like cytoplasmic kinase(RLCK) belonging to the RLK family of proteins and mediates PAMP-triggered stomatal immunity. In turn, bik1 phosphorylates XopR. Furthermore, XopR suppresses PAMP-triggered stomatal closure in transgenic Arabidopsis expressing XopR. In addition, XopR is able to associate with RLCKs other than bik1. These results suggest that XopR likely suppresses plant immunity by targeting bik1 and other RLCKs.

关键词： Xanthomonas effector XopR bik1 immunity

植物受体激酶BAK1介导的细胞死亡调控研究进展

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中国细胞生物学学报 2018年第11期40卷 1944-1951页

作者：冯丽平黎艳蒋亨珂孙歆袁明杜俊波四川农业大学农学院成都611130 四川农业大学生命科学学院雅安625014

植物在生长发育和抵抗逆境时都会发生细胞程序性死亡,植物受体激酶在细胞死亡调控中发挥着十分重要的作用。植物细胞可以通过质膜表面的受体激酶感受细胞间及环境信号,并将信号传递到下游,诱导一系列级联反应,导致细胞程序性死亡。植物... 详细信息

植物在生长发育和抵抗逆境时都会发生细胞程序性死亡,植物受体激酶在细胞死亡调控中发挥着十分重要的作用。植物细胞可以通过质膜表面的受体激酶感受细胞间及环境信号,并将信号传递到下游,诱导一系列级联反应,导致细胞程序性死亡。植物受体激酶BAK1在植物程序性死亡中发挥着关键的作用, BAK1与BRI1、FLS2、BIR1、EFR、bik1等受体激酶互作,识别和转导胞外信号,共同调控细胞死亡。该文以BAK1为中心,综述了近年发现的参与植物细胞死亡调控的BAK1受体激酶复合物介导的信号转导机制,并提出需要深入研究的科学问题。

关键词：植物受体激酶 BAK1 BIR1 FLS2 EFR bik1 细胞死亡