期刊
CELL
卷 185, 期 2, 页码 361-+出版社
CELL PRESS
DOI: 10.1016/j.cell.2021.12.015
关键词
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资金
- Damon Runyon Postdoctoral Fellowship [DRG-2364-19]
- Ruth L. Kirschstein NRSA Postdoctoral Fellowship [F32 GM133096]
- NIH [P41 GM109824, R01 GM112108, R01 GM117212, R01 GM45377, P01 GM121203, R01 GM080139, DP2 GM123494, NSF-1818129]
- Pew Scholars Program [MRI DBI 1920374]
- Stowers Institute for Medical Research
- University of California San Diego
This study provides a structure of the isolated yeast NPC and reveals how flexible connectors tie together different structural and functional layers. It also suggests an evolutionary and mechanistic link between assembly and transport. Additionally, the study identifies three major NPC variants that may signify functional specializations at the nuclear periphery.
Nuclear pore complexes (NPCs) mediate the nucleocytoplasmic transport of macromolecules. Here we provide a structure of the isolated yeast NPC in which the inner ring is resolved by cryo-EM at sub-nanometer resolution to show how flexible connectors tie together different structural and functional layers. These connectors may be targets for phosphorylation and regulated disassembly in cells with an open mitosis. Moreover, some nucleoporin pairs and transport factors have similar interaction motifs, which suggests an evolutionary and mechanistic link between assembly and transport. We provide evidence for three major NPC variants that may foreshadow functional specializations at the nuclear periphery. Cryo-electron tomography extended these studies, providing a model of the in situ NPC with a radially expanded inner ring. Our comprehensive model reveals features of the nuclear basket and central transporter, suggests a role for the lumenal Pom152 ring in restricting dilation, and highlights structural plasticity that may be required for transport.
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