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单分子分析揭示了 FLS2 的磷酸化控制其时空动力学和免疫。

Single-molecule analysis reveals the phosphorylation of FLS2 governs its spatiotemporal dynamics and immunity.

机构信息

State Key Laboratory of Tree Genetics and Breeding, College of Biological Sciences and Technology, Beijing Forestry University, Beijing, China.

National Engineering Research Center of Tree Breeding and Ecological Restoration, College of Biological Sciences and Technology, Beijing Forestry University, Beijing, China.

出版信息

Elife. 2024 Jul 24;12:RP91072. doi: 10.7554/eLife.91072.

DOI:10.7554/eLife.91072
PMID:39046447
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11268883/
Abstract

The FLAGELLIN-SENSITIVE2 (FLS2), a typical receptor kinase, recognizes the conserved 22 amino acid sequence in the N-terminal region of flagellin (flg22) to initiate plant defense pathways, which was intensively studied in the past decades. However, the dynamic regulation of FLS2 phosphorylation at the plasma membrane after flg22 recognition needs further elucidation. Through single-particle tracking, we demonstrated that upon flg22 treatment the phosphorylation of Ser-938 in FLS2 impacts its spatiotemporal dynamics and lifetime. Following Förster resonance energy transfer-fluorescence lifetime imaging microscopy and protein proximity indexes assays revealed that flg22 treatment increased the co-localization of GFP-tagged FLS2/FLS2 but not FLS2 with AtRem1.3-mCherry, a sterol-rich lipid marker, indicating that the phosphorylation of FLS2 affects FLS2 sorting efficiency to Rem1.3-associated nanodomains. Importantly, we found that the phosphorylation of Ser-938 enhanced flg22-induced FLS2 internalization and immune responses, demonstrating that the phosphorylation may activate flg22-triggered immunity through partitioning FLS2 into functional Rem1.3-associated nanodomains, which fills the gap between the FLS2 phosphorylation and FLS2-mediated immunity.

摘要

FLAGELLIN-SENSITIVE2（FLS2）是一种典型的受体激酶，可识别鞭毛蛋白（flg22）N 端区域中保守的 22 个氨基酸序列，从而启动植物防御途径，这在过去几十年中得到了深入研究。然而，在 flg22 识别后，FLS2 在质膜上的磷酸化的动态调节仍需要进一步阐明。通过单颗粒追踪，我们证明了在 flg22 处理后，FLS2 中丝氨酸 938 的磷酸化会影响其时空动力学和寿命。随后进行的Förster 共振能量转移-荧光寿命成像显微镜和蛋白质邻近指数测定表明，flg22 处理增加了 GFP 标记的 FLS2/FLS2 的共定位，但不是 FLS2 与甾醇丰富脂质标记 AtRem1.3-mCherry 的共定位，这表明 FLS2 的磷酸化会影响 FLS2 向 Rem1.3 相关纳米区的分拣效率。重要的是，我们发现丝氨酸 938 的磷酸化增强了 flg22 诱导的 FLS2 内化和免疫反应，表明磷酸化可能通过将 FLS2 分配到功能性 Rem1.3 相关纳米区来激活 flg22 触发的免疫，从而填补了 FLS2 磷酸化和 FLS2 介导的免疫之间的空白。

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