Molecular architecture of the inner ring scaffold of the human nuclear pore complex

Science ◽  
2016 ◽  
Vol 352 (6283) ◽  
pp. 363-365 ◽  
Author(s):  
J. Kosinski ◽  
S. Mosalaganti ◽  
A. von Appen ◽  
R. Teimer ◽  
A. L. DiGuilio ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Molecular Architecture

scholarly journals The Yeast Nuclear Pore Complex

2000 ◽  
Vol 148 (4) ◽  
pp. 635-652 ◽  
Author(s):  
Michael P. Rout ◽  
John D. Aitchison ◽  
Adisetyantari Suprapto ◽  
Kelly Hjertaas ◽  
Yingming Zhao ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nucleocytoplasmic Transport ◽  
Comprehensive Approach ◽  
Nuclear Pore ◽  
Molecular Architecture ◽  
Gating Mechanism ◽  
Molecular Components

An understanding of how the nuclear pore complex (NPC) mediates nucleocytoplasmic exchange requires a comprehensive inventory of the molecular components of the NPC and a knowledge of how each component contributes to the overall structure of this large molecular translocation machine. Therefore, we have taken a comprehensive approach to classify all components of the yeast NPC (nucleoporins). This involved identifying all the proteins present in a highly enriched NPC fraction, determining which of these proteins were nucleoporins, and localizing each nucleoporin within the NPC. Using these data, we present a map of the molecular architecture of the yeast NPC and provide evidence for a Brownian affinity gating mechanism for nucleocytoplasmic transport.

scholarly journals Molecular architecture of the luminal ring of the Xenopus laevis nuclear pore complex

2020 ◽  
Author(s):  
Yanqing Zhang ◽  
Sai Li ◽  
Chao Zeng ◽  
Gaoxingyu Huang ◽  
Xuechen Zhu ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Nuclear Pore Complex ◽  
Electron Tomography ◽  
Structural Features ◽  
Rigid Base ◽  
Nuclear Pore ◽  
Molecular Architecture ◽  
Nuclear Membranes ◽  
Cryo Electron Microscopy ◽  
Cryo Electron Tomography

Nuclear pore complex (NPC) mediates the flow of substances between the nucleus and cytoplasm in eukaryotic cells. Here we report the cryo-electron tomography (cryo-ET) structure of the luminal ring (LR) of the NPC from Xenopus laevis oocyte. The observed key structural features of the LR are independently confirmed by single-particle cryo-electron microscopy (cryo-EM) analysis. The LR comprises eight butterfly-shaped subunits, each containing two symmetric wings. Each wing consists of four elongated, tubular protomers. Within the LR subunit, the eight protomers form a Finger domain, which directly contacts the fusion between the inner and outer nuclear membranes, and a Grid domain, which serves as a rigid base for the Finger domain. Two neighbouring LR subunits interact with each other through the lateral edges of their wings to constitute a Bumper domain, which displays two major conformations and appears to cushion neighbouring NPCs. Our study reveals previously unknown features of the LR and potentially explains the elastic property of the NPC.

scholarly journals Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex

Structure ◽  
2017 ◽  
Vol 25 (3) ◽  
pp. 434-445 ◽  
Author(s):  
Paula Upla ◽  
Seung Joong Kim ◽  
Parthasarathy Sampathkumar ◽  
Kaushik Dutta ◽  
Sean M. Cahill ◽  
...  
Keyword(s):  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Molecular Architecture

scholarly journals Molecular Architecture of the Yeast Nuclear Pore Complex: Localization of Nsp1p Subcomplexes

1998 ◽  
Vol 143 (3) ◽  
pp. 577-588 ◽  
Author(s):  
Birthe Fahrenkrog ◽  
Eduard C. Hurt ◽  
Ueli Aebi ◽  
Nelly Panté
Keyword(s):  
Nuclear Pore Complex ◽  
Protein A ◽  
3D Structure ◽  
Three Dimensional ◽  
Supramolecular Assembly ◽  
Yeast Cells ◽  
Nuclear Pore ◽  
Molecular Architecture ◽  
Gated Channel ◽  
3D Architecture

The nuclear pore complex (NPC), a supramolecular assembly of ∼100 different proteins (nucleoporins), mediates bidirectional transport of molecules between the cytoplasm and the cell nucleus. Extensive structural studies have revealed the three- dimensional (3D) architecture of Xenopus NPCs, and eight of the ∼12 cloned and characterized vertebrate nucleoporins have been localized within the NPC. Thanks to the power of yeast genetics, 30 yeast nucleoporins have recently been cloned and characterized at the molecular level. However, the localization of these nucleoporins within the 3D structure of the NPC has remain elusive, mainly due to limitations of preparing yeast cells for electron microscopy (EM). We have developed a new protocol for preparing yeast cells for EM that yielded structurally well-preserved yeast NPCs. A direct comparison of yeast and Xenopus NPCs revealed that the NPC structure is evolutionarily conserved, although yeast NPCs are 15% smaller in their linear dimensions. With this preparation protocol and yeast strains expressing nucleoporins tagged with protein A, we have localized Nsp1p and its interacting partners Nup49p, Nup57p, Nup82p, and Nic96p by immuno-EM. Accordingly, Nsp1p resides in three distinct subcomplexes which are located at the entry and exit of the central gated channel and at the terminal ring of the nuclear basket.

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