Suppr超能文献

二元细菌蛋白毒素诱导的肌动蛋白细胞骨架解聚对纳米管样突起的形成、Septins组织的调控及囊泡运输的重新导向

Formation of Nanotube-Like Protrusions, Regulation of Septin Organization and Re-guidance of Vesicle Traffic by Depolymerization of the Actin Cytoskeleton Induced by Binary Bacterial Protein Toxins.

作者信息

Schwan Carsten, Aktories Klaus

机构信息

Institute for Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs University of Freiburg, Albertstr. 25, 79104, Freiburg, Germany.

出版信息

Curr Top Microbiol Immunol. 2017;399:35-51. doi: 10.1007/82_2016_25.

Abstract

A large group of bacterial protein toxins, including binary ADP-ribosylating toxins, modify actin at arginine-177, thereby actin polymerization is blocked and the actin cytoskeleton is redistributed. Modulation of actin functions largely affects other components of the cytoskeleton, especially microtubules and septins. Here, recent findings about the functional interconnections of the actin cytoskeleton with microtubules and septins, affected by bacterial toxins, are reviewed.

摘要

一大类细菌蛋白毒素,包括二元ADP核糖基化毒素,会在精氨酸-177位点修饰肌动蛋白,从而阻断肌动蛋白聚合,并使肌动蛋白细胞骨架重新分布。肌动蛋白功能的调节在很大程度上会影响细胞骨架的其他成分,尤其是微管和隔膜蛋白。本文综述了受细菌毒素影响的肌动蛋白细胞骨架与微管和隔膜蛋白之间功能联系的最新研究发现。

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验