顶复合体寄生虫中肌动蛋白的多种功能

IF 4.6 Q2 MATERIALS SCIENCE, BIOMATERIALS ACS Applied Bio Materials Pub Date : 2021-04-22 DOI:10.1111/cmi.13345
Sujaan Das, Johannes Felix Stortz, Markus Meissner, Javier Periz
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引用次数: 8

摘要

细胞骨架蛋白肌动蛋白在真核细胞中含量丰富且保守。它以两种不同的状态发生——球状(g -肌动蛋白)形式,它可以聚合成丝状(f -肌动蛋白)形式,实现各种关键功能,包括细胞质分裂、货物运输和细胞运动。在高等真核生物中,有几种具有几乎相同氨基酸序列的肌动蛋白同种异构体。尽管氨基酸同源性很高,但它们表现出受调控的表达模式和独特的非冗余作用。肌动蛋白同工型的数量和保守序列可能反映了高级真核生物中大量肌动蛋白结合蛋白(ABPs)所施加的选择压力。相比之下,在许多只有少量ABPs的原生动物中,如顶复合体寄生虫,肌动蛋白的调控及其多种功能仍不清楚。本文综述了肌动蛋白在高等真核生物中的调控和生物学功能,并将其与目前在顶复合体中的认识进行了比较。我们讨论了未来的实验,这将有助于我们理解这个迷人的系统在顶复合体中的多重关键作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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The multiple functions of actin in apicomplexan parasites

The cytoskeletal protein actin is highly abundant and conserved in eukaryotic cells. It occurs in two different states- the globular (G-actin) form, which can polymerise into the filamentous (F-actin) form, fulfilling various critical functions including cytokinesis, cargo trafficking and cellular motility. In higher eukaryotes, there are several actin isoforms with nearly identical amino acid sequences. Despite the high level of amino acid identity, they display regulated expression patterns and unique non-redundant roles. The number of actin isoforms together with conserved sequences may reflect the selective pressure exerted by scores of actin binding proteins (ABPs) in higher eukaryotes. In contrast, in many protozoans such as apicomplexan parasites which possess only a few ABPs, the regulatory control of actin and its multiple functions are still obscure. Here, we provide a summary of the regulation and biological functions of actin in higher eukaryotes and compare it with the current knowledge in apicomplexans. We discuss future experiments that will help us understand the multiple, critical roles of this fascinating system in apicomplexans.

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来源期刊
ACS Applied Bio Materials
ACS Applied Bio Materials Chemistry-Chemistry (all)
CiteScore
9.40
自引率
2.10%
发文量
464
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