磷脂酶Dα1衍生的磷脂酸与ABI1磷酸酶2C相互作用并调节脱落酸信号传导。,Proceedings of the National Academy of Sciences of the United States of America

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磷脂酶Dα1衍生的磷脂酸与ABI1磷酸酶2C相互作用并调节脱落酸信号传导。
Proceedings of the National Academy of Sciences of the United States of America ( IF 9.4 ) Pub Date : 2004 Jun 22 , DOI: 10.1073/pnas.0402112101
Wenhua Zhang ₁ , Chunbo Qin ₁ , Jian Zhao ₁ , Xuemin Wang ₁

Affiliation

磷脂酶D（PLD）和蛋白磷酸酶2C（PP2C）都在介导植物对脱落酸（ABA）的反应中发挥作用。在本文中，我们显示PLDα1及其产物磷脂酸（PA）调节PP2C，ABI1，这是拟南芥中ABA响应的负调节剂。与野生型植物相比，来自PLD alpha 1和PLD alpha 1反义植物的T-DNA插入突变体的叶片损失的水分更多。PLD alpha 1-null叶的气孔关闭对ABA不敏感，但由PA促进。在野生型中，ABA处理可促进磷脂酰胆碱的PA升高，但在PLDα1-null细胞中则不会。PLD alpha 1衍生的PA与ABI1结合；通过与植物细胞中的PA和ABI1共沉淀，测量囊泡中PA与ABI1的结合以及测定与固定在滤膜上的PA结合的ABI1，证明了PA-ABI1的结合。缺失和位点特异性突变分析表明，ABI1中的精氨酸73对于PA-ABI1结合至关重要。PA结合会降低ABI1的磷酸酶活性。在PLD alpha 1-null细胞中缺乏ABA诱导的PA产生导致响应ABA的ABI1与质膜的缔合减少。这些结果表明，PLD alpha 1产生的PA抑制了负调控因子ABI1的功能，从而促进了ABA信号传导。将ABI1鉴定为脂质信使PA的直接靶标，可以在两个重要信号酶PLD和PP2C家族之间提供功能上的联系。在PLD alpha 1-null细胞中缺乏ABA诱导的PA产生导致响应ABA的ABI1与质膜的缔合减少。这些结果表明，PLD alpha 1产生的PA抑制了负调控因子ABI1的功能，从而促进了ABA信号传导。将ABI1鉴定为脂质信使PA的直接靶标，可以在两个重要信号酶PLD和PP2C家族之间提供功能上的联系。在PLD alpha 1-null细胞中缺乏ABA诱导的PA产生导致响应ABA的ABI1与质膜的缔合减少。这些结果表明，PLD alpha 1产生的PA抑制了负调控因子ABI1的功能，从而促进了ABA信号传导。将ABI1鉴定为脂质信使PA的直接靶标，可以在两个重要信号酶PLD和PP2C家族之间提供功能上的联系。

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Phospholipase D alpha 1-derived phosphatidic acid interacts with ABI1 phosphatase 2C and regulates abscisic acid signaling.

Phospholipase D (PLD) and protein phosphatase 2C (PP2C) both play a role in mediating plant responses to abscisic acid (ABA). In this article, we show that PLD alpha 1 and its product, phosphatidic acid (PA), regulate a PP2C, ABI1, which is a negative regulator of ABA responses in Arabidopsis. Leaves from a T-DNA insertional mutant of PLD alpha 1 and PLD alpha 1-antisense plants lose more water than do wild-type plants. The stomatal closure of PLD alpha 1-null leaves is insensitive to ABA but is promoted by PA. ABA treatment promotes an increase in PA from phosphatidylcholine in wild type but not in PLD alpha 1-null cells. PLD alpha 1-derived PA binds to ABI1; the PA-ABI1 binding is demonstrated by coprecipitating PA with ABI1 from plant cells, measuring binding of PA from vesicles to ABI1, and assaying ABI1 bound to PA immobilized on a filter. Deletion and site-specific mutational analyses show that arginine 73 in ABI1 is essential for PA-ABI1 binding. PA binding decreases the phosphatase activity of ABI1. The lack of ABA-induced production of PA in PLD alpha 1-null cells results in a decrease in the association of ABI1 with the plasma membrane in response to ABA. These results indicate that PA produced by PLD alpha 1 inhibits the function of the negative regulator ABI1, thus promoting ABA signaling. The identification of ABI1 as a direct target of the lipid messenger PA provides a functional link between the two families of important signaling enzymes, PLD and PP2C.

更新日期：2017-01-31

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