{"title":"MIK2-BAK1 复合物识别 SCOOPs 的机制研究揭示了 N-糖在植物配体-受体-核心受体复合物形成中的作用","authors":"Huimin Wu, Lihao Wan, Zunyong Liu, Yunqing Jian, Chenchen Zhang, Xiakun Mao, Zhiyun Wang, Qiang Wang, Yaxin Hu, Lizhong Xiong, Zhujun Xia, Juan Xue, Shan Li, Ping He, Libo Shan, Shutong Xu","doi":"10.1038/s41477-024-01836-3","DOIUrl":null,"url":null,"abstract":"Ligand-induced receptor and co-receptor heterodimerization is a common mechanism in receptor kinase (RK) signalling activation. SERINE-RICH ENDOGENOUS PEPTIDEs (SCOOPs) mediate the complex formation of Arabidopsis RK MIK2 and co-receptor BAK1, triggering immune responses. Through structural, biochemical and genetic analyses, we demonstrate that SCOOPs use their SxS motif and adjacent residues to bind MIK2 and the carboxy-terminal GGR residues to link MIK2 to BAK1. While N-glycosylation of plant RKs is typically associated with protein maturation, plasma membrane targeting and conformation maintenance, a surprising revelation emerges from our crystal structural analysis of MIK2–SCOOP–BAK1 complexes. Specific N-glycans on MIK2 directly interact with BAK1 upon SCOOP sensing. The absence of N-glycosylation at the specific site in MIK2 neither affects its subcellular localization and protein accumulation in plant cells nor alters its structural conformation, but markedly reduces its affinity for BAK1, abolishing SCOOP-triggered immune responses. This N-glycan-mediated receptor and co-receptor heterodimerization occurs in both Arabidopsis and Brassica napus. Our findings elucidate the molecular basis of SCOOP perception by the MIK2–BAK1 immune complex and underscore the crucial role of N-glycans in plant receptor–coreceptor interactions and signalling activation, shaping immune responses. Wu et al. elucidate the molecular basis for SCOOPs perception by the MIK2–BAK1 immune complex and demonstrate an unexpectedly pivotal role of N-glycans in plant receptor–coreceptor interactions and signalling activation, shaping immune responses.","PeriodicalId":18904,"journal":{"name":"Nature Plants","volume":"10 12","pages":"1984-1998"},"PeriodicalIF":15.8000,"publicationDate":"2024-11-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.com/articles/s41477-024-01836-3.pdf","citationCount":"0","resultStr":"{\"title\":\"Mechanistic study of SCOOPs recognition by MIK2–BAK1 complex reveals the role of N-glycans in plant ligand–receptor–coreceptor complex formation\",\"authors\":\"Huimin Wu, Lihao Wan, Zunyong Liu, Yunqing Jian, Chenchen Zhang, Xiakun Mao, Zhiyun Wang, Qiang Wang, Yaxin Hu, Lizhong Xiong, Zhujun Xia, Juan Xue, Shan Li, Ping He, Libo Shan, Shutong Xu\",\"doi\":\"10.1038/s41477-024-01836-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Ligand-induced receptor and co-receptor heterodimerization is a common mechanism in receptor kinase (RK) signalling activation. SERINE-RICH ENDOGENOUS PEPTIDEs (SCOOPs) mediate the complex formation of Arabidopsis RK MIK2 and co-receptor BAK1, triggering immune responses. Through structural, biochemical and genetic analyses, we demonstrate that SCOOPs use their SxS motif and adjacent residues to bind MIK2 and the carboxy-terminal GGR residues to link MIK2 to BAK1. While N-glycosylation of plant RKs is typically associated with protein maturation, plasma membrane targeting and conformation maintenance, a surprising revelation emerges from our crystal structural analysis of MIK2–SCOOP–BAK1 complexes. Specific N-glycans on MIK2 directly interact with BAK1 upon SCOOP sensing. The absence of N-glycosylation at the specific site in MIK2 neither affects its subcellular localization and protein accumulation in plant cells nor alters its structural conformation, but markedly reduces its affinity for BAK1, abolishing SCOOP-triggered immune responses. This N-glycan-mediated receptor and co-receptor heterodimerization occurs in both Arabidopsis and Brassica napus. Our findings elucidate the molecular basis of SCOOP perception by the MIK2–BAK1 immune complex and underscore the crucial role of N-glycans in plant receptor–coreceptor interactions and signalling activation, shaping immune responses. Wu et al. elucidate the molecular basis for SCOOPs perception by the MIK2–BAK1 immune complex and demonstrate an unexpectedly pivotal role of N-glycans in plant receptor–coreceptor interactions and signalling activation, shaping immune responses.\",\"PeriodicalId\":18904,\"journal\":{\"name\":\"Nature Plants\",\"volume\":\"10 12\",\"pages\":\"1984-1998\"},\"PeriodicalIF\":15.8000,\"publicationDate\":\"2024-11-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.nature.com/articles/s41477-024-01836-3.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature Plants\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.nature.com/articles/s41477-024-01836-3\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"PLANT SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature Plants","FirstCategoryId":"99","ListUrlMain":"https://www.nature.com/articles/s41477-024-01836-3","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
Mechanistic study of SCOOPs recognition by MIK2–BAK1 complex reveals the role of N-glycans in plant ligand–receptor–coreceptor complex formation
Ligand-induced receptor and co-receptor heterodimerization is a common mechanism in receptor kinase (RK) signalling activation. SERINE-RICH ENDOGENOUS PEPTIDEs (SCOOPs) mediate the complex formation of Arabidopsis RK MIK2 and co-receptor BAK1, triggering immune responses. Through structural, biochemical and genetic analyses, we demonstrate that SCOOPs use their SxS motif and adjacent residues to bind MIK2 and the carboxy-terminal GGR residues to link MIK2 to BAK1. While N-glycosylation of plant RKs is typically associated with protein maturation, plasma membrane targeting and conformation maintenance, a surprising revelation emerges from our crystal structural analysis of MIK2–SCOOP–BAK1 complexes. Specific N-glycans on MIK2 directly interact with BAK1 upon SCOOP sensing. The absence of N-glycosylation at the specific site in MIK2 neither affects its subcellular localization and protein accumulation in plant cells nor alters its structural conformation, but markedly reduces its affinity for BAK1, abolishing SCOOP-triggered immune responses. This N-glycan-mediated receptor and co-receptor heterodimerization occurs in both Arabidopsis and Brassica napus. Our findings elucidate the molecular basis of SCOOP perception by the MIK2–BAK1 immune complex and underscore the crucial role of N-glycans in plant receptor–coreceptor interactions and signalling activation, shaping immune responses. Wu et al. elucidate the molecular basis for SCOOPs perception by the MIK2–BAK1 immune complex and demonstrate an unexpectedly pivotal role of N-glycans in plant receptor–coreceptor interactions and signalling activation, shaping immune responses.
期刊介绍:
Nature Plants is an online-only, monthly journal publishing the best research on plants — from their evolution, development, metabolism and environmental interactions to their societal significance.