在秀丽隐杆线虫中,α微管蛋白乙酰转移酶atat-2与klp-4基因相互作用。

microPublication biology Pub Date : 2025-04-11 eCollection Date: 2025-01-01 DOI:10.17912/micropub.biology.001536
Claire E Reist, Michael D Webb, Cortlen M Mathews, Jay N Pieczynski
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引用次数: 0

摘要

微管动力学在一定程度上受翻译后修饰的调控,包括乙酰化。关于微管乙酰化状态及其如何影响运动蛋白功能之间的关系,特别是在体内,我们所知甚少。我们将微管动力学的药理学操作与遗传学方法相结合,通过对秀丽隐杆线虫进行一系列的灭威敏感性试验,我们证明了α微管蛋白乙酰转移酶atat-2和运动蛋白klp-4之间存在特定的遗传相互作用。我们的工作强调了体内运动蛋白活性和微管蛋白代码之间的相互作用,并为这两个平行但相关的细胞过程的未来工作奠定了基础。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The alpha tubulin acetyltransferase atat-2 genetically interacts with klp-4 in C. elegans.

Microtubules dynamics are in part regulated by post-translational modification, including acetylation. Little is known about the relationship between microtubule acetylation status and how this affects kinesin function, especially in vivo . Using a series of aldicarb sensitivity assays in C. elegans where we combined pharmacological manipulation of microtubule dynamics with genetic approaches, we demonstrate a specific genetic interaction between the alpha tubulin acetyltransferase atat-2 and the kinesin motor klp-4 . Our work highlights interactions between kinesin activity and the tubulin code in vivo and lays the foundation of future work on these two parallel, yet related processes in cells.

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