Zanetti Giulia, Prinz Simone, Daum Sebastian, Meister Annette, Schekman Randy, Bacia Kirsten, Briggs John A G
Department of Molecular and Cell Biology , University of California, Berkeley , Berkeley , United States.
Elife. 2013 Sep 17;2:e00951. doi: 10.7554/eLife.00951.
Coat protein complex II (COPII) mediates formation of the membrane vesicles that export newly synthesised proteins from the endoplasmic reticulum. The inner COPII proteins bind to cargo and membrane, linking them to the outer COPII components that form a cage around the vesicle. Regulated flexibility in coat architecture is essential for transport of a variety of differently sized cargoes, but structural data on the assembled coat has not been available. We have used cryo-electron tomography and subtomogram averaging to determine the structure of the complete, membrane-assembled COPII coat. We describe a novel arrangement of the outer coat and find that the inner coat can assemble into regular lattices. The data reveal how coat subunits interact with one another and with the membrane, suggesting how coordinated assembly of inner and outer coats can mediate and regulate packaging of vesicles ranging from small spheres to large tubular carriers. DOI:http://dx.doi.org/10.7554/eLife.00951.001.
II型被膜小泡蛋白复合物(COPII)介导从内质网输出新合成蛋白质的膜泡形成。COPII内部蛋白与货物和膜结合,将它们与在囊泡周围形成笼子的COPII外部组件相连。被膜结构中受调控的灵活性对于各种不同大小货物的运输至关重要,但尚未获得已组装被膜的结构数据。我们使用冷冻电子断层扫描和亚断层图平均法来确定完整的、膜组装的COPII被膜的结构。我们描述了外部被膜的一种新排列方式,并发现内部被膜可以组装成规则晶格。这些数据揭示了被膜亚基如何相互作用以及与膜相互作用,表明内部和外部被膜的协同组装如何介导和调节从小球体到大型管状载体等不同囊泡的包装。DOI:http://dx.doi.org/10.7554/eLife.00951.001 。