Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly.,Nature Structural & Molecular Biology

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Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly.
Nature Structural & Molecular Biology ( IF 12.5 ) Pub Date : 2019-10-03 , DOI: 10.1038/s41594-019-0292-0
Kyle L Morris _{1,

2} , Joseph R Jones ₁ , Mary Halebian ₁ , Shenping Wu _{3,

4} , Michael Baker _{1,

5} , Jean-Paul Armache _{6,

7} , Amaurys Avila Ibarra ₈ , Richard B Sessions ₈ , Alexander D Cameron ₁ , Yifan Cheng _{3,

6} , Corinne J Smith ₁

Affiliation

Clathrin forms diverse lattice and cage structures that change size and shape rapidly in response to the needs of eukaryotic cells during clathrin-mediated endocytosis and intracellular trafficking. We present the cryo-EM structure and molecular model of assembled porcine clathrin, providing insights into interactions that stabilize key elements of the clathrin lattice, namely, between adjacent heavy chains, at the light chain-heavy chain interface and within the trimerization domain. Furthermore, we report cryo-EM maps for five different clathrin cage architectures. Fitting structural models to three of these maps shows that their assembly requires only a limited range of triskelion leg conformations, yet inherent flexibility is required to maintain contacts. Analysis of the protein-protein interfaces shows remarkable conservation of contact sites despite architectural variation. These data reveal a universal mode of clathrin assembly that allows variable cage architecture and adaptation of coated vesicle size and shape during clathrin-mediated vesicular trafficking or endocytosis.

中文翻译：

多笼结构的冷冻电镜揭示了网格蛋白自组装的通用模式。

网格蛋白形成多种晶格和笼状结构，在网格蛋白介导的内吞作用和细胞内运输过程中响应真核细胞的需要而迅速改变大小和形状。我们展示了组装的猪网格蛋白的低温-EM 结构和分子模型，提供了对稳定网格蛋白晶格关键元素的相互作用的见解，即相邻重链之间、轻链-重链界面处和三聚化域内的相互作用。此外，我们报告了五种不同网格蛋白笼架构的冷冻电镜图。将结构模型拟合到其中三个地图表明，它们的组装只需要有限范围的 triskelion 腿构象，但需要固有的灵活性来保持接触。蛋白质 - 蛋白质界面的分析表明，尽管结构变化，但接触位点的显着保护。这些数据揭示了网格蛋白组装的通用模式，该模式允许在网格蛋白介导的囊泡运输或内吞作用期间改变笼结构并适应涂层囊泡的大小和形状。

更新日期：2019-10-03

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