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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Phospholipase Dα1 -derived phosphatidic acid interacts with ABI1 phosphatase 2C and regulates abscisic acid signaling
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Phospholipase Dα1 -derived phosphatidic acid interacts with ABI1 phosphatase 2C and regulates abscisic acid signaling

机译: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

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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 PLDαl 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 PLDα1 and PLDα1-antisense plants lose more water than do wild-type plants. The stomatal closure of PLDα1-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 PLDα1-null cells. PLDα1-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 PLDα1-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 PLDα1 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.
机译:磷脂酶D(PLD)和蛋白磷酸酶2C(PP2C)都在介导植物对脱落酸(ABA)的反应中起作用。在本文中,我们显示PLDα1及其产物磷脂酸(PA)调节PP2C,ABI1,ABI1是拟南芥中ABA反应的负调节剂。与野生型植物相比,来自PLDα1和PLDα1反义植物的T-DNA插入突变体的叶片损失的水分更多。 PLDα1-无效叶片的气孔关闭对ABA不敏感,但被PA促进。 ABA处理在野生型中促进磷脂酰胆碱的PA升高,但在PLDα1无细胞中则不促进。来自PLDα1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。缺乏ABA诱导的PLDα1无效细胞中PA的产生导致响应于ABA的ABI1与质膜的缔合减少。这些结果表明由PLDα1产生的PA抑制了负调节剂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,可在两个重要信号酶PLD和PP2C家族之间建立功能联系。

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