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| 1 | Plant pattern-recognition receptors controlling innate immunity显示文摘Plants are exposed to numerous potential pathogenic microbes. To counter the threat, plants have evolved diverse patternrecognition receptors(PRRs), which are receptor kinases(RKs) and receptor proteins(RPs) specialized to detect conserved pathogen/microbe-associated molecular patterns(PAMPs/MAMPs). Although only a handful of RKs and RPs are known PRRs,they belong to the receptor-like kinase(RLK) and receptor-like protein(RLP) superfamilies that undergo lineage-specific expansion, suggesting that many of these RLKs and RLPs are potential PRRs. Analyses of existing PRRs have uncovered ligand-induced RLK-RK or RLK-RP oligomerization as a common mechanism for immune activation. PRRs can recruit additional components to form dynamic receptor complexes, which mediate specific cellular responses. Detailed analyses of these components are shedding light on molecular mechanisms underlying the regulation of PRR activity and downstream signaling. | Lei Li Yufei Yu Zhaoyang Zhou Jian-Min Zhou | 2016 | Science China(Life Sciences)2016，59，9： | 16 |
| 2 | Structural insights into the negative regulation of BRI1 signaling by BRI1-interacting protein BKI1显示文摘Brassinosteroids (BR ) 是在植物生长和开发有关键角色的必要类固醇荷尔蒙。BR 被房间表面察觉像受体的 kinase brassinosteroid 感觉迟钝 1 (BRI1 ) 。当 BR 不在时, BRI1 的 cytosolic kinase 领域(KD ) 被它的汽车禁止的 carboxyl 终点,以及由与禁止者蛋白质交往禁止, BRI1 kinase 禁止者 1 (BKI1 ) 。对 BRI1 的细胞外的域有约束力的 BR 怎么导致 BKI1 的 KD 和分离的激活进 cytosol,仍然保持不清楚。这里,我们报导在有交往的肽的建筑群的 BRI1 KD 的水晶结构源于 BKI1。我们也提供生物化学的证据那联系 BRI1 的 kinase (BAK1 ) 1 在开始 BR 发信号起一个必要作用。BRI1 和 BAK1 ectodomains 的类固醇依赖者 heterodimerization 为与 BKI1 和 transphosphorylation 竞争在正确取向带他们的细胞质的 KD。 | Jie Wang Jianjun Jiang Jue Wang Lei Chen Shi-Long Fan Jia-Wei Wu Xuelu Wang Zhi-Xin Wang | 2014 | Cell Research2014，24，11： | 12 |
| 3 | BAK1 Directly Regulates Brassinosteroid Perception and BRI1 Activation显示文摘Plants utilize plasma membrane-localized receptor-like kinases(RLKs)to sense extracellular signals to coordinate growth,development,and innate immune responses.BAK1 regulates multiple signaling pathways acting as a co-receptor of several distinct ligand-binding RLKs.It has been debated whether BAK1 serves as an essential regulatory component or only a signal amplifer without pathway specifcity.This issue has been clarifed recently.Genetic and structural analyses indicated that BAK1 and its homologs play indispensible roles in mediating brassinosteroid(BR)signaling pathway by directly perceiving the ligand BR and activating the receptor of BR,BRI1.The mechanism revealed by these studies now serves as a paradigm for how a pair of RLKs can function together in ligand binding and subsequent initiation of signaling. | Kai He Shengbao Xu Jia Li | 2013 | Journal of Integrative Plant Biology2013，55，12： | 10 |
| 4 | 蛋白磷酸化修饰在植物-病原微生物互作中的作用研究进展显示文摘蛋白磷酸化修饰是植物细胞信号调控的普遍机制。植物-病原微生物互作过程中,关键调控蛋白的磷酸化状态影响免疫信号的激活。多种病原微生物通过干扰宿主蛋白的磷酸化状态攻击免疫系统,以提高致病性。该文对植物免疫调控过程中关键元件的磷酸化修饰及其在免疫信号中的调控作用进行了综述。研究植物-病原菌互作过程中关键蛋白的磷酸化修饰,有助于深入探讨植物-病原微生物互作的分子机理。该文将为寻找广谱抗病的新途径提供理论依据。 | 刘雅琼 侯岁稳 | 2019 | 植物学报2019，0，2： | 8 |
| 5 | 植物受体激酶BAK1研究进展显示文摘植物受体激酶BAK1在多个信号转导路径上独立的多角色功能,成为拟南芥受体激酶610个成员中最受关注的成员之一。BAK1是一个典型的富亮氨酸重复序列的跨膜受体激酶,属于LRR-RKⅡ家族,在结构上由胞外结合域、跨膜区以及胞内激酶结构域三部分构成。最初BAK1被鉴定为BRI1和FLS2的双元受体,分别参与调控植物油菜素内酯BR的信号转导及病原相关模式分子PAMPs引发的免疫反应,近期又有多个BAK1的互作组分被相继发现,如EFR、AvrPto、PEPR1/2、PUB13、BIR1、BON1等。该文从BAK1的分子结构,BAK1所在SERKs家族的功能冗余,对油菜素内酯路径的信号调控,参与病菌识别防御反应的先天免疫和调控细胞凋亡等方面对近年来国内外的相关研究进展进行综述,以明确目前研究所面临的问题。 | 田荣 杨勇 王晓峰 | 2014 | 西北植物学报2014，34，3： | 7 |
| 6 | Ligand Perception,Activation,and Early Signaling of Plant Steroid Receptor Brassinosteroid Insensitive 1显示文摘Leucine-rich repeat receptor-like kinases(LRR-RLKs)belong to a large group of cell surface proteins involved in many aspects of plant development and environmental responses in both monocots and dicots.Brassinosteroid insensitive 1(BRI1),a member of the LRR X subfamily,was frst identifed through several forward genetic screenings for mutants insensitive to brassinosteroids(BRs),which are a class of plant-specifc steroid hormones.Since its identifcation,BRI1 and its homologs had been proved as receptors perceiving BRs and initiating BR signaling.The co-receptor BRI1-associated kinase 1and its homologs,and other BRI1 interacting proteins such as its inhibitor BRI1 kinase inhibitor 1(BKI1)were identifed by genetic and biochemical approaches.The detailed mechanisms of BR perception by BRI1 and the activation of BRI1receptor complex have also been elucidated.Moreover,several mechanisms for termination of the activated BRI1 signaling were also discovered.In this review,we will focus on the recent advances on the mechanism of BRI1 phosphorylation and activation,the regulation of its receptor complex,the structure basis of BRI1ectodomain and BR recognition,its direct substrates,and the termination of the activated BRI1 receptor complex. | Jianjun JiangWang Chi ZhangWang Xuelu Wang | 2013 | Journal of Integrative Plant Biology2013，55，12： | 6 |
| 7 | Structural analysis of receptor-like kinase SOBIR1 reveals mechanisms that regulate its phosphorylation-dependent activation显示文摘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 transduction.Both LRR-RLKs and LRR-RLPs rely on regulatory LRR-RLKs to initiate downstream signaling pathways.BRASSINOSTEROID 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 functions.Although the regulatory mechanism of BAK1 activation has been studied in detail,the activation mechanism of SOBIR1 remains poorly understood.Here,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 helices.Biochemical 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 phosphorylation.Further functional analysis confirmed the importance of Thr529 and the β3-αC loop for the SOBIR1-induced cell death response in Nicotiana benthamiana.Taken 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. | Xue Wei Yulu Wang Su Zhang Tianyi Gu Gabryel Steinmetz Haiyan Yu Guoguang Guo Xin Liu Shilong Fan Fengzhong Wang Yangnan Gu Fengjiao Xin | 2022 | Plant Communications2022，3，2： | 2 |
| 8 | Specifying the role of BAK1-interacting receptor-like kinase 3 in brassinosteroid signaling显示文摘Brassinosteroids(BR) are involved in the control of several developmental processes ranging from root elongation to senescence and adaptation to environmental cues. Thus, BR perception and signaling have to be precisely regulated. One regulator is BRI1-associated kinase 1(BAK1)-interacting receptor-like kinase 3(BIR3). In the absence of BR, BIR3 forms complexes with BR insensitive 1(BRI1) and BAK1.However, the biophysical and energetic requirements for complex formation in the absence of the ligand have yet to be determined. Using computational modeling, we simulated the potential complexes between the cytoplasmic domains of BAK1, BRI1 and BIR3. Our calculations and experimental data confirm the interaction of BIR3 Rewith BAK1 and BRI1, with the BAK1 BIR3 interaction clearly favored. Furthermore, we demonstrate that BIR3 and BRI1 share the same interaction site with BAK1. This suggests a competition between BIR3 and BRI1 for binding to BAK1, which results in preferential binding of BIR3 to BAK1 in the absence of the ligand thereby preventing the active participation of BAK1 in BR signaling. Our model also suggests that BAK1 and BRI1 can interact even while BAK1 is in complex with BIR3 at an additional binding site of BAK1 that does not allow active BR signaling. | Ruth Groβeholz Anna Feldman-Salit Friederike Wanke Sarina Schulze Nina Glockner Birgit Kemmerling Klaus Harter Ursula Kummer | 2020 | Journal of Integrative Plant Biology2020，62，4： | 1 |
| 9 | CRISPR/Cas9技术在水稻类受体激酶基因OsBAK1L突变体制备中的应用显示文摘植物类受体激酶在植物生长发育及响应外界环境信号刺激中具有重要作用,为了进一步研究水稻类受体激酶OsBAK1L的功能,我们利用CRISPR/Cas9技术对该基因进行定点编辑。OsBAK1L定位在细胞膜上且该基因预测编码蛋白包含三个功能结构域:胞外LRR结构域、跨膜结构域及胞内激酶域。为了进一步理解该蛋白不同结构域上的功能,我们分别在胞外LRR结构域(Target 1)和胞内激酶域(Target 2)上设计该基因定点编辑靶点。将合成的靶位点序列插入入门载体CH,然后与表达载体Cas9进行重组。重组载体通过农杆菌介导方法转入野生型水稻9522中,2个构建分别获得26棵和12棵潮霉素抗性植株。通过对转基因植株的测序分析,找到了3棵和2棵序列发生变化的杂合T_0代植株。T_0代杂合植株自交分离分别获得T_1代两靶位点处纯合子突变体,靶位点1处纯合子突变体株系缺失5个碱基,靶位点2处纯合子突变体株系插入1个碱基,均可造成该基因转录本翻译提前终止。该基因不同结构域上突变体的获得为进一步研究该基因功能提供了重要且稳定的遗传材料。 | 韩娇娇 余君萍 宋明 梁婉琪 | 2018 | 基因组学与应用生物学2018，37，2： | 1 |
| 10 | Identifi cation and functional analysis of phosphorylation residues of the Arabidopsis BOTRYTIS-INDUCED KINASE1显示文摘Arabidopsis BOTRYTIS-INDUCED KINASE1(BIK1)is a receptor-like cytoplasmic kinase acting early in multiple signaling pathways important for plant growth and innate immunity.It 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 residues.Here,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 time.The 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 residues.We also mapped new sites of FLS2 phosphorylation by BIK1,which are different from those by BAK1.These 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. | Jinhua Xu Xiaochao Wei Limin Yan Dan Liu Yuanyuan Ma Yu Guo Chune Peng Honggang Zhou Cheng Yang Zhiyong Lou Wenqing Shui | 2013 | Protein & Cell2013，4，10： | 0 |
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