DYNAMIN-RELATED PROTEIN DRP1A functions with DRP2B in plant growth, flg22-immune responses, and endocytosis
DYNAMIN-RELATED PROTEIN DRP1A functions with DRP2B in plant growth, flg22-immune responses, and endocytosis
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DOI：
10.1093/plphys/kiab024
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发表时间：
2021-02-03
期刊：
影响因子：
7.4
通讯作者：
Heese, Antje
中科院分区：
文献类型：
--
作者：
Ekanayake, Gayani;Smith, John M.;Heese, Antje
配体诱导的免疫受体FLAGELLIN SENSING2 （FLS2）的内吞作用对于维持其在质膜（PM）中的适当丰度，从而启动并随后下调细胞对细菌鞭毛蛋白或flg22肽的免疫反应至关重要。然而，控制FLS2的PM丰度的分子成分大部分仍然未知。在这里，我们发现拟南芥（拟南芥）动力蛋白相关蛋白1a （DRP1A）是植物特异性大动力蛋白gtpase家族的成员，是配体诱导FLS2内吞及其在flg22信号传导和对丁香假单胞菌pv免疫中的生理作用的关键因素。番茄叶片DC3000细菌。值得注意的是，drp1a单突变体表现出与先前报道的另一种动力蛋白相关蛋白DRP2B突变体相似的flg22缺陷，DRP2B先前被证明与drp1a共定位。我们的研究还揭示了DRP1A和DRP2B在植物生长发育中的协同作用，因为DRP1A和DRP2B双突变体表现出严重的根和子叶发育不良，以及细胞形状、细胞分裂和幼苗致死缺陷。此外，在flg22处理之前，drp1a和drp2b双突变体在PM中过度积累FLS2，并表现出对配体诱导的FLS2内吞作用的阻断，这表明drp1a和DRP1B在控制FLS2在PM中的丰度方面具有联合作用。然而，在drp1a和drp2b双突变体中，FLS2稳态PM积累的增加并没有导致flg22反应的增加。我们认为DRP1A和DRP2B对PM相关的FLS2水平的调控很重要，而FLS2是获得启动不同flg22反应的信号能力所必需的，可能通过调节特定PM结构域的脂质环境。
Ligand-induced endocytosis of the immune receptor FLAGELLIN SENSING2 (FLS2) is critical for maintaining its proper abundance in the plasma membrane (PM) to initiate and subsequently down regulate cellular immune responses to bacterial flagellin or flg22-peptide. The molecular components governing PM abundance of FLS2, however, remain mostly unknown. Here, we identified Arabidopsis (Arabidopsis thaliana) DYNAMIN-RELATED PROTEIN1A (DRP1A), a member of a plant-specific family of large dynamin GTPases, as a critical contributor to ligand-induced endocytosis of FLS2 and its physiological roles in flg22-signaling and immunity against Pseudomonas syringae pv. tomato DC3000 bacteria in leaves. Notably, drp1a single mutants displayed similar flg22-defects as those previously reported for mutants in another dynamin-related protein, DRP2B, that was previously shown to colocalize with DRP1A. Our study also uncovered synergistic roles of DRP1A and DRP2B in plant growth and development as drp1a drp2b double mutants exhibited severely stunted roots and cotyledons, as well as defective cell shape, cytokinesis, and seedling lethality. Furthermore, drp1a drp2b double mutants hyperaccumulated FLS2 in the PM prior to flg22-treatment and exhibited a block in ligand-induced endocytosis of FLS2, indicating combinatorial roles for DRP1A and DRP1B in governing PM abundance of FLS2. However, the increased steady-state PM accumulation of FLS2 in drp1a drp2b double mutants did not result in increased flg22 responses. We propose that DRP1A and DRP2B are important for the regulation of PM-associated levels of FLS2 necessary to attain signaling competency to initiate distinct flg22 responses, potentially through modulating the lipid environment in defined PM domains.