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首页> 外文期刊>Cell motility and the cytoskeleton >Rho signaling in Entamoeba histolytica modulates actomyosin-dependent activities stimulated during invasive behavior.
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Rho signaling in Entamoeba histolytica modulates actomyosin-dependent activities stimulated during invasive behavior.

机译：溶组织性变形杆菌中的Rho信号调节在侵袭行为中刺激的肌动球蛋白依赖性活性。

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Interaction of Entamoeba histolytica trophozoites with target cells and substrates activates signaling pathways in the parasite. Phosphorylation cascades triggered by phospho-inositide and adenyl-cyclase-dependent pathways modulate reorganization of the actin cytoskeleton to form structures that facilitate adhesion. In contrast, little is known about participation of Rho proteins and Rho signaling in actin rearrangements. We report here the in vivo expression of at least one Rho protein in trophozoites, whose activation induced actin reorganization and actin-myosin interaction. Antibodies to EhRhoA1 recombinant protein mainly localized Rho in the cytosol of nonactivated amoebae, but it was translocated to vesicular membranes and to some extent to the plasma membrane after treatment with lysophosphatidic acid (LPA), a specific agonist of Rho activation. Activated Rho was identified in LPA-treated trophozoites. LPA induced striking polymerization of actin into distinct dynamic structures. Disorganizationof these structures by inhibition of Rho effector, Rho-kinase (ROCK), and by ML-7, an inhibitor of myosin light chain kinase dependent phosphorylation of myosin light chain, suggested that the actin structures also contained myosin. LPA stimulated concanavalin-A-mediated formation of caps, chemotaxis, invasion of extracellular matrix substrates, and erythrophagocytosis, but not binding to fibronectin. ROCK inhibition impaired LPA-stimulated functions and to some extent adhesion to fibronectin. Similar results were obtained with ML-7. These data suggest the presence and operation of Rho-signaling pathways in E. histolytica, that together with other, already described, signaling routes modulate actomyosin-dependent motile processes, particularly stimulated during invasive behavior.
机译：变形虫变形虫滋养体与靶细胞和底物的相互作用激活了寄生虫中的信号通路。由磷酸肌醇和腺苷酸环化酶依赖性途径触发的磷酸化级联反应可调节肌动蛋白细胞骨架的重组，从而形成促进粘附的结构。相反，关于Rho蛋白和Rho信号参与肌动蛋白重排的了解甚少。我们在这里报告至少一种Rho蛋白在滋养体中的体内表达，其活化诱导肌动蛋白重组和肌动蛋白-肌球蛋白相互作用。 EhRhoA1重组蛋白的抗体主要将Rho定位在未激活的变形虫的胞质溶胶中，但在用Rho激活的特异性激动剂溶血磷脂酸（LPA）处理后，它转移到了水泡膜，并在一定程度上转移到了质膜。在LPA处理的滋养体中鉴定出活化的Rho。 LPA诱导肌动蛋白惊人的聚合成不同的动态结构。通过抑制Rho效应子，Rho激酶（ROCK）以及通过抑制肌球蛋白轻链激酶依赖性肌球蛋白轻链磷酸化的ML-7，这些结构的紊乱表明肌动蛋白结构也含有肌球蛋白。 LPA刺激伴刀豆球蛋白A介导的帽形成，趋化作用，细胞外基质底物的侵袭和红细胞吞噬作用，但不与纤连蛋白结合。 ROCK抑制作用削弱了LPA刺激的功能，并在一定程度上粘附于纤连蛋白。使用ML-7可获得类似的结果。这些数据表明溶组织性大肠杆菌中Rho信号通路的存在和运行，以及其他已经描述的信号传导途径，调节了放线菌素依赖性运动过程，特别是在侵入性行为中受到刺激。

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