美国加州理工学院
结合生化重组、高分辨率结构测定、对接低温电子断层扫描重建和生理学验证，研究人员阐明了进化保守的连接-支架结构，产生了人类核孔复合体（NPC）约64兆道尔顿对称核心的近原子复合结构。虽然连接体通常起到固定的作用，但NPC的连接-支架提供了其中央运输通道的可逆收缩和扩张以及横向通道的出现所必需的可塑性和稳健性。这些结果大大推进了NPC对称核心的结构特征，为未来的功能研究提供了基础。
据悉，NPC介导大分子的核细胞质运输。尽管NPC对称核心中的结构化支架核蛋白的排列已经确定，但它们与多价非结构的连接核蛋白的凝聚力仍然难以确定。
附：英文原文
Title: Architecture of the linker-scaffold in the nuclear pore
Author: Stefan Petrovic, Dipanjan Samanta, Thibaud Perriches, Christopher J. Bley, Karsten Thierbach, Bonnie Brown, Si Nie, George W. Mobbs, Taylor A. Stevens, Xiaoyu Liu, Giovani Pinton Tomaleri, Lucas Schaus, André Hoelz
Issue&Volume: 2022-06-10
Abstract: Nuclear pore complexes (NPCs) mediate the nucleocytoplasmic transport of macromolecules. Although the arrangement of the structured scaffold nucleoporins in the NPC’s symmetric core has been determined, their cohesion by multivalent unstructured linker nucleoporins has remained elusive. Combining biochemical reconstitution, high-resolution structure determination, docking into cryo–electron tomographic reconstructions, and physiological validation, we elucidated the architecture of the evolutionarily conserved linker-scaffold, yielding a near-atomic composite structure of the human NPC’s ~64-megadalton symmetric core. Whereas linkers generally play a rigidifying role, the linker-scaffold of the NPC provides the plasticity and robustness necessary for the reversible constriction and dilation of its central transport channel and the emergence of lateral channels. Our results substantially advance the structural characterization of the NPC symmetric core, providing a basis for future functional studies.
DOI: abm9798
Source: https://www.science.org/doi/10.1126/science.abm9798