在水解后状态下,膜结合的胺的冷EM结构为膜裂变做准备
John R Jimah1, Nidhi Kundu1, Abigail E Stanton1
1Laboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
动氨酸形成螺旋状聚合物,在内细胞分裂过程中收缩和切断囊泡. 新的冷EM结构揭示了动力胺.
科学领域:
- 生物化学 生物化学
- 细胞生物学 细胞生物学
- 结构生物学 结构生物学
背景情况:
- 动氨酸是一种GTPase,对内细胞囊泡形成至关重要.
- 之前的原子模型在早期收缩阶段捕获了动力素.
- 活组件在GTP水解后的状态仍然没有特征.
研究的目的:
- 为了确定GTP后氨酸水解的原子结构.
- 在细胞环境中可视化动组装状态.
主要方法:
- 使用冷电子显微镜 (cryo-EM) 来解析原子结构.
- 脂质管模仿了内细胞囊的子,用于体外组装.
- 低温电子断层扫描 (cryo-ET) 在HeLa细胞中可视化了dynamin.
主要成果:
- 确定了在超狭窄,GDP-bound状态下的动力素的原子结构.
- 发动机组装成一个双启动螺旋,具有3.4纳米光度,准备进行裂变.
- 冷-ET揭示了细胞中的多种动螺旋组件,先于膜裂变.
结论:
- GDP-bound状态代表了动介导膜收缩的晚期阶段.
- 在细胞膜裂变事件中,dynamin表现出形状灵活性.
- 这些发现为囊泡分裂的最后步骤提供了原子洞察力.
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