Arabidopsis ADR1 helper NLR immune receptors localize and function at the plasma membrane in a phospholipid dependent manner
Arabidopsis ADR1 helper NLR immune receptors localize and function at the plasma membrane in a phospholipid dependent manner
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DOI：
10.1111/nph.17788
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发表时间：
2021-10-23
期刊：
影响因子：
9.4
通讯作者：
El Kasmi, Farid
中科院分区：
文献类型：
--
作者：
Saile, Svenja C.;Ackermann, Frank M.;El Kasmi, Farid
核苷酸结合的富亮氨酸重复序列受体（NLR）的激活导致免疫和局部细胞死亡。NLR细胞死亡活性需要寡聚化，并且在某些情况下需要质膜（PM）定位。缺乏预测的跨膜结构域或可识别的脂化基序的NLR的PM定位的确切机制仍然难以捉摸。我们使用共聚焦显微镜，遗传编码的分子工具和蛋白质-脂质覆盖测定，以确定是否PM本地化的拟南芥HeLo-/RPW 8-样域的“助手”NLR（RNL）家族的成员介导的带负电荷的磷脂的PM的相互作用。我们的研究结果表明，PM定位和稳定的一些RNL和CC型NLR（CNL）依赖于直接与PM磷脂的相互作用。耗尽磷脂酰肌醇-4-磷酸从PM导致错误定位的分析NLR，因此抑制其细胞死亡活性。我们进一步证明同性恋和异性恋协会的RNL家族的成员。我们的研究结果提供了新的见解NLR本地化的分子机制，并定义了一个重要的作用，磷脂的CNL和RNL PM本地化，因此，他们的功能。我们提出，RNL与阴离子PM磷脂相互作用，RNL介导的细胞死亡和免疫反应发生在PM。
Activation of nucleotide-binding leucine-rich repeat receptors (NLRs) results in immunity and a localized cell death. NLR cell death activity requires oligomerization and in some cases plasma membrane (PM) localization. The exact mechanisms underlying PM localization of NLRs lacking predicted transmembrane domains or recognizable lipidation motifs remain elusive. We used confocal microscopy, genetically encoded molecular tools and protein-lipid overlay assays to determine whether PM localization of members of the Arabidopsis HeLo-/RPW8-like domain 'helper' NLR (RNL) family is mediated by the interaction with negatively charged phospholipids of the PM. Our results show that PM localization and stability of some RNLs and one CC-type NLR (CNL) depend on the direct interaction with PM phospholipids. Depletion of phosphatidylinositol-4-phosphate from the PM led to a mis-localization of the analysed NLRs and consequently inhibited their cell death activity. We further demonstrate homo- and hetero-association of members of the RNL family. Our results provide new insights into the molecular mechanism of NLR localization and defines an important role of phospholipids for CNL and RNL PM localization and consequently, for their function. We propose that RNLs interact with anionic PM phospholipids and that RNL-mediated cell death and immune responses happen at the PM.