PKD is recruited to sites of actin remodelling at the leading edge and negatively regulates cell migration
PKD is recruited to sites of actin remodelling at the leading edge and negatively regulates cell migration
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DOI：
10.1016/j.febslet.2007.07.079
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发表时间：
2007-09-04
期刊：
影响因子：
3.5
通讯作者：
Hausser, Angelika
中科院分区：
文献类型：
--
作者：
Eiseler, Tim;Schmid, Michael A.;Hausser, Angelika
蛋白激酶D（PKD）参与细胞形状、粘附和迁移的调节。在迁移细胞的前沿，活性PKD与F-肌动蛋白、Arp 3和corpine共定位。血小板衍生生长因子（PDGF）激活PKD并将激酶募集到前沿，表明PKD在肌动蛋白重塑中的作用。为了支持这一点，PKD直接与F-肌动蛋白相互作用，并在体外磷酸化coronin。干扰PKD功能的显性负PKD的过表达或PKD特异性siRNA增强细胞迁移，而细胞过度表达PKD野生型显示迁移潜力降低。总之，这些数据揭示了PKD在细胞迁移中的负调节功能。(c)2007年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Protein kinase D (PKD) has been implicated in the regulation of cell shape, adhesion, and migration. At the leading edge of migrating cells active PKD co-localizes with F-actin, Arp3 and cortactin. Platelet derived growth factor (PDGF) activates PKD and recruits the kinase to the leading edge, suggesting a role for PKD in actin remodelling. In support of this, PKD directly interacts with F-actin and phosphorylates cortactin in vitro. Interference with PKD function by overexpression of a dominant negative PKD or by PKD-specific siRNA enhanced cell migration, whereas cells overexpressing PKD wild type displayed reduced migratory potential. Taken together, these data reveal a negative regulatory function of PKD in cell migration. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.