Solving the nuclear pore puzzle.

Solving the nuclear pore puzzle.
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解决核孔之谜。

DOI:
10.1126/science.abq4792
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发表时间:
2022
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Schwartz,ThomasU
Schwartz,ThomasU
中科院分区:
--
文献类型:
--
作者:
Schwartz,ThomasU

文献摘要

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在真核细胞中,基因组被隔离在细胞核中,双层核膜(NE)将其与细胞质隔开。大分子的运输通过核孔复合体(∼)发生,它在NP200-2000位置穿透NE(-)。高达40 kDa的离子和分子通过鼻咽癌扩散,而较大的货物选择性地与可溶的核运输因子结合,通过中央∼通道运输。但目前还不清楚NPC是如何准确地控制大量不同底物的运输,包括可溶性蛋白质、嵌入的膜蛋白、RNA,甚至一些病毒衣壳。在本期的第1174、1175、1176、1177和1178页上,Bleyer等人、Petrovicet等人、Mosalagantiet等人、Chuet等人和Fontanaet等人现在分别以前所未有的细节提供了NPC是如何构建的分子结构。这些发现将使进一步剖析NPC的许多功能成为可能。
In eukaryotic cells, the genome is sequestered in the nucleus, shielded from the cytoplasm by the double-layered nuclear envelope (NE). Transport of macromolecules across the NE occurs through nuclear pore complexes (NPCs), which perforate the NE at ∼200 to 2000 positions (–). Ions and molecules up to ∼40 kDa diffuse through NPCs, whereas larger cargo selectively associate with soluble nuclear transport factors to be ferried through the central NPC channel . But it has been unclear how NPCs exactly control the transport of a vast array of different substrates, including soluble proteins, embedded membrane proteins, RNAs, and even some viral capsids. On pages 1174, 1175, 1176, 1177, and 1178 of this issue, Bleyet al., Petrovicet al., Mosalagantiet al., Zhuet al., and Fontanaet al., respectively, now provide molecular structures, in unprecedented detail, of how NPCs are built. These findings will enable approaches to further dissect the many NPC functions.