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Review
. 2023 May 1;435(9):168051.
doi: 10.1016/j.jmb.2023.168051. Epub 2023 Mar 17.

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

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Free article
Review

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

Linhua Tai et al. J Mol Biol. .
Free article

Abstract

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.

Keywords: cryo-electron microscopy; cryo-electron tomography; in situ structure; nuclear pore complex.

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Conflict of interest statement

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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