N-糖基化促进植物细胞表面受体的激活

IF 15.8 1区 生物学 Q1 PLANT SCIENCES
Fangshuai Jia, Yu Xiao, Yaojie Feng, Jinghui Yan, Mingzhu Fan, Yue Sun, Shijia Huang, Weiguo Li, Tian Zhao, Zhifu Han, Shuguo Hou, Jijie Chai
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引用次数: 0

摘要

植物受体激酶(RKs)是跨膜信号传导的关键,涉及包括植物免疫在内的各种生物过程。雄性发现者1-互作受体样激酶2(MIK2)是一种独特的RK,它能识别称为ERINE-RICH ENDOGENOUS PEPTIDEs(SCOOPs)的免疫调节肽家族,并激活模式触发的免疫反应。然而,人们对 SCOOP 识别和 MIK2 激活的确切机制仍然知之甚少。在这里,我们以 3.34 Å 的分辨率展示了由 MIK2 的胞外富含亮氨酸的重复序列 (LRR)、SCOOP12 和共受体 BAK1 的胞外 LRR (BAK1LRR) 组成的三元复合物的低温电子显微镜结构。该结构揭示了 MIK2LRR 中的 DNHH 基序在特异性识别 SCOOP12 高度保守的 SxS 基序方面起着关键作用。此外,该结构还表明 MIK2LRRAsn410 上的 N-聚糖直接与 BAK1LRR 的 N 端封顶区相互作用。糖基化位点 MIK2LRRN410D 的突变完全取消了 MIK2LRR 和 BAK1LRR 之间不依赖于 SCOOP12 的相互作用,并大大影响了 MIK2LRR-SCOOP12-BAK1LRR 复合物的组装。支持 N410-糖基化生物学相关性的是,MIK2N410D 会大大损害植物中 SCOOP12 触发的免疫反应。总之,这些发现阐明了 MIK2 识别 SCOOP 的松散特异性机制,并揭示了 LRR-RK 的 N-糖基化修饰促进受体活化的一种前所未有的机制。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

N-glycosylation facilitates the activation of a plant cell-surface receptor

N-glycosylation facilitates the activation of a plant cell-surface receptor

N-glycosylation facilitates the activation of a plant cell-surface receptor
Plant receptor kinases (RKs) are critical for transmembrane signalling involved in various biological processes including plant immunity. MALE DISCOVERER1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) is a unique RK that recognizes a family of immunomodulatory peptides called SERINE-RICH ENDOGENOUS PEPTIDEs (SCOOPs) and activates pattern-triggered immunity responses. However, the precise mechanisms underlying SCOOP recognition and activation of MIK2 remain poorly understood. Here we present the cryogenic electron microscopy structure of a ternary complex consisting of the extracellular leucine-rich repeat (LRR) of MIK2 (MIK2LRR), SCOOP12 and the extracellular LRR of the co-receptor BAK1 (BAK1LRR) at a resolution of 3.34 Å. The structure reveals that a DNHH motif in MIK2LRR plays a critical role in specifically recognizing the highly conserved SxS motif of SCOOP12. Furthermore, the structure demonstrates that N-glycans at MIK2LRRAsn410 directly interact with the N-terminal capping region of BAK1LRR. Mutation of the glycosylation site, MIK2LRRN410D, completely abolishes the SCOOP12-independent interaction between MIK2LRR and BAK1LRR and substantially impairs the assembly of the MIK2LRR–SCOOP12–BAK1LRR complex. Supporting the biological relevance of N410-glycosylation, MIK2N410D substantially compromises SCOOP12-triggered immune responses in plants. Collectively, these findings elucidate the mechanism underlying the loose specificity of SCOOP recognition by MIK2 and reveal an unprecedented mechanism by which N-glycosylation modification of LRR-RK promotes receptor activation. This study demonstrates a crucial role of N-glycosylation in activating a receptor-like kinase by promoting its interaction with co-receptors.
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来源期刊
Nature Plants
Nature Plants PLANT SCIENCES-
CiteScore
25.30
自引率
2.20%
发文量
196
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.
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