肌动蛋白:肌动蛋白在非肌肉细胞中的未聚合形式

U Lindberg, L Carlsson, F Markey, L E Nyström
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引用次数: 0

摘要

一些证据表明,在非肌肉细胞中存在未聚合的肌动蛋白。超微结构检查显示各种肌动蛋白丝束和肌动蛋白在一个有争议的组织状态。有观点认为,这种至少部分存在于质膜附近的物质代表未聚合的肌动蛋白,而不是单个肌动蛋白细丝的随机排列。在细胞周期中肌动蛋白丝束的重排,以及对实验操作的响应,表明了通过聚合-解聚合循环的丝的周转。在肌动蛋白聚合的条件下,从非肌肉细胞中提取的提取物仍然含有可观的单体肌动蛋白。对来自各种来源的纯化的抗聚合肌动蛋白的研究表明,存在一种小蛋白质,它特异性地与肌动蛋白结合并阻止聚合。在文章的最后一部分,我们扩展了这种辅助蛋白是体内非聚合和聚合肌动蛋白之间调节交换的中心控制元件的想法。
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The unpolymerised form of actin in non-muscle cells.

Several lines of evidence point to the existence of unpolymerised actin in non-muscle cells. Ultrastructural examination reveals both a variety of actin filament bundles and actin in a controversial organisational state. Arguments are cited that this material, which at least in part is found close to the plasma membrane, represents unpolymerised actin rather than a random array of single actin filaments. The rearrangement of actin filament bundles during the cell cycle, and in response to experimental manipulation, suggests a turnover of filaments by a polymerisation-depolymerisation cycle. Extracts made from non-muscle cells under conditions where muscle actin would polymerise still contain appreciable fractions of monomeric actin. Studies on purified polymerisation-resistant actin from a variety of sources reveal the presence of a small protein which binds specifically to actin and prevents polymerisation. In the last section of the article, we expand the idea that this auxiliary protein is a central control element in the regulated exchange between non-polymerised and polymerised actin in vivo.

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