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首页> 外文期刊>The Plant Cell >C2-Domain Abscisic Acid-Related Proteins Mediate the Interaction of PYR/PYL/RCAR Abscisic Acid Receptors with the Plasma Membrane and Regulate Abscisic Acid Sensitivity in Arabidopsis
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C2-Domain Abscisic Acid-Related Proteins Mediate the Interaction of PYR/PYL/RCAR Abscisic Acid Receptors with the Plasma Membrane and Regulate Abscisic Acid Sensitivity in Arabidopsis

机译：C2-域脱落酸相关蛋白介导拟南芥中PYR / PYL / RCAR脱落酸受体与质膜的相互作用并调节脱落酸敏感性。

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摘要

Membrane-delimited abscisic acid (ABA) signal transduction plays a critical role in early ABA signaling, but the molecular mechanisms linking core signaling components to the plasma membrane are unclear. We show that transient calcium-dependent interactions of PYR/PYL ABA receptors with membranes are mediated through a 10-member family of C2-domain ABA-related (CAR) proteins in Arabidopsis thaliana. Specifically, we found that PYL4 interacted in an ABAindependent manner with CAR1 in both the plasma membrane and nucleus of plant cells. CAR1 belongs to a plantspecific gene family encoding CAR1 to CAR10 proteins, and bimolecular fluorescence complementation and coimmunoprecipitation assays showed that PYL4-CAR1 as well as other PYR/PYL-CAR pairs interacted in plant cells. The crystal structure of CAR4 was solved, which revealed that, in addition to a classical calcium-dependent lipid binding C2 domain, a specific CAR signature is likely responsible for the interaction with PYR/PYL receptors and their recruitment to phospholipid vesicles. This interaction is relevant for PYR/PYL function and ABA signaling, since different car triple mutants affected in CAR1, CAR4, CAR5, and CAR9 genes showed reduced sensitivity to ABA in seedling establishment and root growth assays. In summary, we identified PYR/PYL-interacting partners that mediate a transient Ca2+-dependent interaction with phospholipid vesicles, which affects PYR/PYL subcellular localization and positively
机译：膜分隔脱落酸（ABA）信号转导在早期ABA信号传导中起关键作用，但将核心信号传导成分连接到质膜的分子机制尚不清楚。我们显示，PYR / PYL ABA受体与膜的瞬时钙依赖性相互作用是通过拟南芥中的C2域ABA相关（CAR）蛋白的10个成员族介导的。具体而言，我们发现PYL4在植物细胞的质膜和细胞核中都以ABA独立的方式与CAR1相互作用。 CAR1属于植物特异性基因家族，编码CAR1至CAR10蛋白，并且双分子荧光互补和共免疫沉淀分析表明PYL4-CAR1以及其他PYR / PYL-CAR对在植物细胞中相互作用。解析了CAR4的晶体结构，这表明，除了经典的钙依赖性脂质结合C2结构域外，特定的CAR标记还可能负责与PYR / PYL受体的相互作用以及它们对磷脂小泡的募集。这种相互作用与PYR / PYL功能和ABA信号有关，因为在CAR1，CAR4，CAR5和CAR9基因中受影响的不同汽车三联突变体在苗期建立和根系生长测定中对ABA的敏感性降低。总而言之，我们确定了PYR / PYL相互作用的伙伴，它们介导与磷脂囊泡的Ca2 +依赖的短暂相互作用，从而影响PYR / PYL亚细胞定位并产生积极影响

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