University of Missouri-Columbia, Division of Biochemistry, Interdisciplinary Plant Group (IPG), Columbia, MO, U.S.A.
University of Missouri-Columbia, Division of Plant Sciences & Technology, Columbia, MO, U.S.A.
Mol Plant Microbe Interact. 2023 Apr;36(4):201-207. doi: 10.1094/MPMI-10-22-0207-FI. Epub 2023 Apr 13.
In eukaryotes, dynamins and dynamin-related proteins (DRPs) are high-molecular weight GTPases responsible for mechanochemical fission of organelles or membranes. Of the six DRP subfamilies in , AtDRP1 and AtDRP2 family members serve as endocytic accessory proteins in clathrin-mediated endocytosis. Most studies have focused on AtDRP1A and AtDRP2B as critical modulators of plant pattern-triggered immunity (PTI) against pathogenic, flagellated pv. DC3000 bacteria and immune signaling in response to the bacterial flagellin peptide flg22. Much less is known about AtDRP2A, the closely related paralog of AtDRP2B. AtDRP2A and AtDRP2B are the only classical, or , dynamins in , based on their evolutionary conserved domain structure with mammalian dynamins functioning in endocytosis. AtDRP2B but not AtDRP2A is required for robust ligand-induced endocytosis of the receptor kinase FLAGELLIN SENSING2 for dampening of early flg22 signaling. Here, we utilized null mutants to identify AtDRP2A as a positive contributor to effective PTI against pv. DC3000 bacteria, consistent with reduced () messenger RNA accumulation. We provide evidence that AtDRP2A is a novel modulator of late flg22 signaling, contributing positively to gene induction but negatively to polyglucan callose deposition. AtDRP2A has no apparent roles in flg22-elicited mitogen-activated protein kinase defense marker gene induction. In summary, this study adds the evolutionary conserved dynamin AtDRP2A to a small group of vesicular trafficking proteins with roles as non-canonical contributors in immune responses, likely due to modulating one or both the localization and activity of multiple different proteins with distinct contributions to immune signaling. [Formula: see text] Copyright © 2023 The Author(s). This is an open access article distributed under the CC BY-NC-ND 4.0 International license.
在真核生物中，动力蛋白和动力蛋白相关蛋白（DRP）是负责细胞器或膜机械化学分裂的高分子重量 GTP 酶。在 中，有六个 DRP 亚家族，AtDRP1 和 AtDRP2 家族成员作为网格蛋白介导的内吞作用中的内吞辅助蛋白。大多数研究集中在 AtDRP1A 和 AtDRP2B 作为植物模式触发免疫（PTI）对致病性、鞭毛状 pv 的关键调节剂。 DC3000 细菌和对细菌鞭毛肽 flg22 的免疫信号的反应。关于 AtDRP2A，AtDRP2B 的密切相关的同源物，了解得要少得多。AtDRP2A 和 AtDRP2B 是唯一的经典或经典，动力蛋白，基于它们与哺乳动物动力蛋白在胞吞作用中起作用的进化保守结构域结构。AtDRP2B 但不是 AtDRP2A 是受体激酶 FLAGELLIN SENSING2 引起的配体诱导的内吞作用所必需的，用于减弱早期 flg22 信号。在这里，我们利用 缺失突变体来鉴定 AtDRP2A 作为对 pv 的有效 PTI 的积极贡献者。 DC3000 细菌，与减少一致 ()信使 RNA 积累。我们提供的证据表明，AtDRP2A 是晚期 flg22 信号的新型调节剂，对 基因诱导呈正贡献，但对多聚糖 callose 沉积呈负贡献。AtDRP2A 在 flg22 诱导的丝裂原活化蛋白激酶防御标记基因诱导中没有明显作用。总之，这项研究将进化保守的动力蛋白 AtDRP2A 添加到一小群具有免疫反应中非典型贡献者作用的囊泡转运蛋白中，可能是由于调节一个或多个对免疫信号有不同贡献的不同蛋白质的定位和活性。[公式：见正文]版权所有 2023 年作者。这是一个开放获取的文章，根据 CC BY-NC-ND 4.0 国际许可发布。
