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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >A pre-embedding immunogold approach reveals localization of myosin VI at the ultrastructural level in the actin cones that mediate Drosophila spermatid individualization
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A pre-embedding immunogold approach reveals localization of myosin VI at the ultrastructural level in the actin cones that mediate Drosophila spermatid individualization

机译：嵌入前的免疫金方法揭示了肌球蛋白VI在肌动蛋白视锥细胞的超微结构水平上的定位，介导果蝇精子个体化。

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摘要

Stable actin structures play important roles in the development and specialization of differentiated cells. How these structures form, are organized, and are used to mediate physiological processes is not well understood in most cases. In Drosophila testis, stable actin structures, called actin cones, mediate spermatid individualization, a large-scale cellular remodeling process. These actin cones are composed of two structural domains, a front meshwork and a rear region of parallel bundles. Myosin VI is an important player in proper actin cone organization and function. Myosin VI localizes to the cones' fronts and its specific localization is required for proper actin cone formation and function during individualization. To understand how these structures are organized and assembled, ultrastructural studies are important to reveal both organization of actin and the precise localization of actin regulators relative to regions with different filament organizations. In the present work, we have developed a novel pre-embedding immunogold-silver labeling method for high-resolution analysis of protein distribution in actin structures which allowed both satisfactory antibody labeling and good ultrastructural preservation. Electron microscopic studies revealed that myosin VI accumulated at the extreme leading edge of the actin cone and preferentially localized throughout the front meshwork of the cone where branched actin filaments were most concentrated. No myosin VI labeling was found adjacent to the membranes along the length of the cone or connecting neighboring cones. This method has potential to reveal important information about precise relationships between actin-binding proteins, membranes, and different types of actin structures.
机译：稳定的肌动蛋白结构在分化细胞的发育和特化中起重要作用。在大多数情况下，这些结构是如何形成，组织和用于介导生理过程的尚不清楚。在果蝇睾丸中，称为肌动蛋白视锥的稳定肌动蛋白结构介导精子个体化，这是大规模的细胞重塑过程。这些肌动蛋白视锥细胞由两个结构域组成，前部网状结构和平行束的后部区域。肌球蛋白VI是适当的肌动蛋白视锥细胞组织和功能的重要参与者。肌球蛋白VI定位于视锥的前端，在具体化过程中，其特定的定位是正确的肌动蛋白视锥形成和功能所必需的。为了了解这些结构是如何组织和组装的，超微结构研究对于揭示肌动蛋白的组织以及肌动蛋白调节剂相对于具有不同细丝组织的区域的精确定位至关重要。在目前的工作中，我们已经开发了一种新型的预包埋免疫金银标记方法，用于高分辨率分析肌动蛋白结构中的蛋白质分布，该方法可以实现令人满意的抗体标记和良好的超微结构保存。电子显微镜研究表明，肌球蛋白VI聚集在肌动蛋白视锥的最前端，并优先分布在视锥的前网状结构中，分支肌动蛋白丝最集中。在沿锥体长度的膜附近或连接相邻锥体的膜附近未发现肌球蛋白VI标记。这种方法有可能揭示有关肌动蛋白结合蛋白，膜和不同类型的肌动蛋白结构之间精确关系的重要信息。

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