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首页> 外文期刊>IUBMB life >Holding back the microfilamentuStructural insights into actin and theTI Holding back the microfilamentuStructural insights into actin and the actin-monomer-binding proteins of apicomplexan parasites
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Holding back the microfilamentuStructural insights into actin and theTI Holding back the microfilamentuStructural insights into actin and the actin-monomer-binding proteins of apicomplexan parasites

机译:阻止微丝对肌动蛋白和TI的结构学见解阻止微丝对肌动蛋白和apicomplexan寄生虫的肌动蛋白-单体结合蛋白的见解。

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摘要

Parasites from the phylum Apicomplexa are responsible for several major diseases of man, including malaria and toxoplasmosis. These highly motile protozoa use a conserved actomyosin-based mode of movement to power tissue traversal and host cell invasion. The mode termed as gliding motility relies on the dynamic turnover of actin, whose polymerisation state is controlled by a markedly limited number of identifiable regulators when compared with other eukaryotic cells. Recent studies of apicomplexan actin regulator structurein particular those of the core triad of monomer-binding proteins, actin-depolymerising factor/cofilin, cyclase-associated protein/Srv2, and profilinhave provided new insights into possible mechanisms of actin regulation in parasite cells, highlighting divergent structural features and functions to regulators from other cellular systems. Furthermore, the unusual nature of apicomplexan actin itself is increasingly coming into the spotlight. Here, we review recent advances in understanding of the structure and function of actin and its regulators in apicomplexan parasites. In particular we explore the paradox between there being an abundance of unpolymerised actin, its having a seemingly increased potential to form filaments relative to vertebrate actin, and the apparent lack of visible, stable filaments in parasite cells. 2012 IUBMB IUBMB Life, 2012
机译:蚜虫门的寄生虫是人类几种主要疾病的病因,包括疟疾和弓形虫病。这些高度活动的原生动物使用保守的基于肌动球蛋白的运动方式来推动组织的遍历和宿主细胞的侵袭。称为滑行运动的模式依赖于肌动蛋白的动态更新,与其他真核细胞相比,肌动蛋白的聚合状态受明显数量有限的可识别调节剂控制。 apicomplexan肌动蛋白调节剂结构的最新研究,特别是单体结合蛋白,肌动蛋白解聚因子/ cofilin,环化酶相关蛋白/ Srv2和脯氨酸蛋白三联体核心三联体的结构,为寄生虫细胞中肌动蛋白调节的可能机制提供了新见解,突出了分歧其他蜂窝系统的调节器的结构特征和功能。此外,apicomplexan肌动蛋白本身的非同寻常的性质越来越受到关注。在这里,我们审查了解肌动蛋白及其在apicomplexan寄生虫中的调节剂的结构和功能的最新进展。特别是,我们探索了一个矛盾,即存在大量未聚合的肌动蛋白,相对于脊椎动物肌动蛋白而言,其似乎具有增加的形成细丝的潜力,以及在寄生虫细胞中明显缺乏可见的,稳定的细丝。 2012 IUBMB IUBMB人寿,2012年

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