Cryo-electron Microscopy Reveals the Structure of the Nuclear Pore Complex

被引:14
|
作者
Tai, Linhua [1 ,2 ]
Yin, Guoliang [1 ,2 ]
Sun, Fei [1 ,2 ,3 ,4 ]
Zhu, Yun [1 ]
机构
[1] Chinese Acad Sci, Inst Biophys, CAS Ctr Excellence Biomacromol, Natl Key Lab Biomacromol, Beijing 100101, Peoples R China
[2] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[3] Chinese Acad Sci, Inst Biophys, Ctr Biol Imaging, Beijing 100101, Peoples R China
[4] Guangzhou Regenerat Med & Hlth Guangdong Lab, Bioland Lab, Guangzhou 510005, Guangdong, Peoples R China
基金
中国国家自然科学基金;
关键词
cryo-electron microscopy; nuclear pore complex; cryo-electron tomography; in situ structure; SCANNING-ELECTRON-MICROSCOPY; MESSENGER-RNA EXPORT; MOLECULAR ARCHITECTURE; ATOMIC-STRUCTURE; FIELD-EMISSION; INNER RING; CRYSTAL-STRUCTURE; FG-NUCLEOPORINS; FUNCTIONAL-ANALYSIS; CYTOPLASMIC FACE;
D O I
10.1016/j.jmb.2023.168051
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The nuclear pore complex (NPC) is a giant protein assembly that penetrates the double layers of the nuclear membrane. The overall structure of the NPC has approximately eightfold symmetry and is formed by approximately 30 nucleoporins. The great size and complexity of the NPC have hindered the study of its structure for many years until recent breakthroughs were achieved by integrating the latest high -resolution cryo-electron microscopy (cryo-EM), the emerging artificial intelligence-based modeling and all other available structural information from crystallography and mass spectrometry. Here, we review our latest knowledge of the NPC architecture and the history of its structural study from in vitro to in situ with progressively improved resolutions by cryo-EM, with a particular focus on the latest subnanometer-resolution structural studies. The future directions for structural studies of NPCs are also discussed.(c) 2023 The Author(s). Published by Elsevier Ltd.
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收藏
页数:18
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