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Structure and gating of the nuclear pore complex

Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we analyse the structure of the NPC scaffold and permeability barrier, by reconstructing the Xen...

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Autores principales: Eibauer, Matthias, Pellanda, Mauro, Turgay, Yagmur, Dubrovsky, Anna, Wild, Annik, Medalia, Ohad
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Pub. Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4491817/
https://www.ncbi.nlm.nih.gov/pubmed/26112706
http://dx.doi.org/10.1038/ncomms8532
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author Eibauer, Matthias
Pellanda, Mauro
Turgay, Yagmur
Dubrovsky, Anna
Wild, Annik
Medalia, Ohad
author_facet Eibauer, Matthias
Pellanda, Mauro
Turgay, Yagmur
Dubrovsky, Anna
Wild, Annik
Medalia, Ohad
author_sort Eibauer, Matthias
collection PubMed
description Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we analyse the structure of the NPC scaffold and permeability barrier, by reconstructing the Xenopus laevis oocyte NPC from native nuclear envelopes up to 20 Å resolution by cryo-electron tomography in conjunction with subtomogram averaging. In addition to resolving individual protein domains of the NPC constituents, we propose a model for the architecture of the molecular gate at its central channel. Furthermore, we compare and contrast this native NPC structure to one that exhibits reduced transport activity and unveil the spatial properties of the NPC gate.
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spelling pubmed-44918172015-07-08 Structure and gating of the nuclear pore complex Eibauer, Matthias Pellanda, Mauro Turgay, Yagmur Dubrovsky, Anna Wild, Annik Medalia, Ohad Nat Commun Article Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we analyse the structure of the NPC scaffold and permeability barrier, by reconstructing the Xenopus laevis oocyte NPC from native nuclear envelopes up to 20 Å resolution by cryo-electron tomography in conjunction with subtomogram averaging. In addition to resolving individual protein domains of the NPC constituents, we propose a model for the architecture of the molecular gate at its central channel. Furthermore, we compare and contrast this native NPC structure to one that exhibits reduced transport activity and unveil the spatial properties of the NPC gate. Nature Pub. Group 2015-06-26 /pmc/articles/PMC4491817/ /pubmed/26112706 http://dx.doi.org/10.1038/ncomms8532 Text en Copyright © 2015, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Eibauer, Matthias
Pellanda, Mauro
Turgay, Yagmur
Dubrovsky, Anna
Wild, Annik
Medalia, Ohad
Structure and gating of the nuclear pore complex
title Structure and gating of the nuclear pore complex
title_full Structure and gating of the nuclear pore complex
title_fullStr Structure and gating of the nuclear pore complex
title_full_unstemmed Structure and gating of the nuclear pore complex
title_short Structure and gating of the nuclear pore complex
title_sort structure and gating of the nuclear pore complex
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4491817/
https://www.ncbi.nlm.nih.gov/pubmed/26112706
http://dx.doi.org/10.1038/ncomms8532
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