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[C][W]
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[C][W]
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DOI：
10.1105/tpc.114.129973
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发表时间：
2014-12
期刊：
影响因子：
11.6
通讯作者：
Lesia Rodriguez;Miguel González-Guzmán;M. Díaz;Américo Rodrigues;A. C. Izquierdo-Garcia;Marta Peirats-Llobet-Marta-Pei
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文献类型：
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作者：
Lesia Rodriguez;Miguel González-Guzmán;M. Díaz;Américo Rodrigues;A. C. Izquierdo-Garcia;Marta Peirats-Llobet-Marta-Pei
脱落酸受体作为质膜中的外周蛋白的亚细胞定位是由C2结构域脱落酸相关蛋白以钙依赖性方式介导的。脱落酸（阿坝）信号转导在早期阿坝信号转导中起着关键作用，但核心信号组分与质膜之间的分子机制尚不清楚。我们表明，瞬时钙依赖的PYR/PYL阿坝受体与膜的相互作用介导的C2结构域ABA相关（CAR）蛋白在拟南芥的10个成员的家庭。具体而言，我们发现PYL 4在植物细胞的质膜和细胞核中以ABA非依赖性方式与CAR 1相互作用。CAR 1属于植物特异性基因家族，编码CAR 1至CAR 10蛋白，双分子荧光互补和免疫共沉淀试验表明PYL 4-CAR 1以及其他PYR/PYL-CAR对在植物细胞中相互作用。解析了CAR 4的晶体结构，这揭示了除了经典的钙依赖性脂质结合C2结构域之外，特异性CAR特征可能负责与PYR/PYL受体的相互作用及其向磷脂囊泡的募集。这种相互作用与PYR/PYL功能和阿坝信号传导相关，因为在CAR 1、CAR 4、CAR 5和CAR 9基因中受影响的不同car三重突变体在幼苗建立和根生长测定中显示出对阿坝的敏感性降低。总之，我们确定了PYR/PYL相互作用伙伴，它们介导与磷脂囊泡的短暂Ca 2+依赖性相互作用，这会影响PYR/PYL亚细胞定位并正调节阿坝信号传导。
Subcellular localization of abscisic acid receptors as peripheral proteins in the plasma membrane is mediated in a calcium-dependent manner by C2-domain abscisic acid-related proteins. 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 ABA-independent manner with CAR1 in both the plasma membrane and nucleus of plant cells. CAR1 belongs to a plant-specific 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 regulates ABA signaling.