Capping of actin filaments by vinculin activated by the Shigella IpaA carboxyl-terminal domain
Capping of actin filaments by vinculin activated by the Shigella IpaA carboxyl-terminal domain
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DOI：
10.1016/j.febslet.2007.01.057
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发表时间：
2007-03-06
期刊：
影响因子：
3.5
通讯作者：
Van Nhieu, Guy Tran
中科院分区：
文献类型：
--
作者：
Ramarao, Nalini;Le Clainche, Christophe;Van Nhieu, Guy Tran
志贺氏菌是细菌性痢疾的病原体，它会侵入上皮细胞。在细菌与细胞接触时，III型细菌效应蛋白IpaA会与细胞骨架蛋白纽蛋白结合，以促进细菌有效摄取所需的肌动蛋白重组。我们发现，IpaA的最后74个C末端残基（A559）与人纽蛋白（HV）结合，并促进其与肌动蛋白丝的结合。聚合实验表明，A559足以诱导HV依赖的肌动蛋白丝带刺端的部分封端。这些结果表明，IpaA通过调节纽蛋白的带刺端封端活性来调控志贺氏菌入侵部位的肌动蛋白聚合/解聚。（c）2007欧洲生物化学学会联合会。由爱思唯尔出版集团出版。保留所有权利。
Shigella, the causative agent of bacillary dysentery, invades epithelial cells. Upon bacterial-cell contact, the type III bacterial effector IpaA binds to the cytoskeletal protein vinculin to promote actin reorganization required for efficient bacterial uptake. We show that the last 74 C-terminal residues of IpaA (A559) bind to human vinculin (HV) and promotes its association with actin filaments. Polymerisation experiments demonstrated that A559 was sufficient to induce HV-dependent partial capping of the barbed ends of actin filaments. These results suggest that IpaA regulates actin polymerisation/depolymerisation at sites of Shigella invasion by modulating the barbed end capping activity of vinculin. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.