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首页> 外文期刊>Cellular Signalling >Interaction of PLD1b with actin in antigen-stimulated mast cells
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Interaction of PLD1b with actin in antigen-stimulated mast cells

机译：PLD1b与肌动蛋白在抗原刺激的肥大细胞中的相互作用

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Phosphatidic acid, the product of phospholipase D catalysed phosphatidylcholine hydrolysis is an important signalling molecule that has been implicated in regulation of actin cytoskeleton remodelling and secretion from mast cells. We show that human PLD1b (hPLD1b) is an actin-binding protein and the N-terminus is predominantly involved in this interaction. Protein kinase C (PKC) is a major upstream regulator of PLD activity and PKC phosphorylation sites have been identified within the N-terminus of PLDIb at serine 2 and threonine 147. Over-expression of wild type hPLD1b in mast cells showed that antigen stimulation significantly enhanced co-localisation of PLD1b with actin structures. Mutation of serine 2 to alanine abolished antigen-induced co-localisation whereas mutation of threonine 147 had less dramatic effects on co-localisation. The absence of co-localisation of PLDIb (S2A) with actin coincides with a significant decrease in PLD activity in cells expressing the PLD1b (S2A) mutant. In resting RBL-2H3 cells, mutation of serine 2 to aspartate resulted in constitutive co-localisation of PLD with the actin cytoskeleton, coincident with restored PLD activity. These results reveal that serine 2 is an important regulatory site involved in controlling PLD enzyme activity and the interaction between PLD and actin. (c) 2006 Elsevier Inc. All rights reserved.
机译：磷脂酶D催化的磷脂酰胆碱水解产物磷脂酸是一种重要的信号分子，已参与调节肌动蛋白细胞骨架重塑和肥大细胞分泌。我们显示人类PLD1b（hPLD1b）是肌动蛋白结合蛋白和N端主要参与此相互作用。蛋白激酶C（PKC）是PLD活性的主要上游调节剂，已经在PLDIb的N末端丝氨酸2和苏氨酸147的N末端发现了PKC磷酸化位点。肥大细胞中野生型hPLD1b的过表达表明抗原刺激显着增强的PLD1b与肌动蛋白结构的共定位。丝氨酸2突变为丙氨酸消除了抗原诱导的共定位，而苏氨酸147的突变对共定位的影响较小。 PLDIb（S2A）与肌动蛋白的共定位不存在与表达PLD1b（S2A）突变体的细胞中PLD活性的显着降低相吻合。在静止的RBL-2H3细胞中，丝氨酸2突变为天冬氨酸导致PLD与肌动蛋白细胞骨架组成性共定位，与恢复的PLD活性一致。这些结果表明，丝氨酸2是参与控制PLD酶活性以及PLD和肌动蛋白之间相互作用的重要调控位点。 （c）2006 Elsevier Inc.保留所有权利。

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