The Yeast Nuclear Pore Complex: Composition, Architecture, and Transport Mechanism

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...

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Autores principales: Rout, Michael P., Aitchison, John D., Suprapto, Adisetyantari, Hjertaas, Kelly, Zhao, Yingming, Chait, Brian T.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2000
Materias:
Original Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2169373/
https://www.ncbi.nlm.nih.gov/pubmed/10684247
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author Rout, Michael P.
Aitchison, John D.
Suprapto, Adisetyantari
Hjertaas, Kelly
Zhao, Yingming
Chait, Brian T.
author_facet Rout, Michael P.
Aitchison, John D.
Suprapto, Adisetyantari
Hjertaas, Kelly
Zhao, Yingming
Chait, Brian T.
author_sort Rout, Michael P.
collection PubMed
description 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.
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spelling pubmed-21693732008-05-01 The Yeast Nuclear Pore Complex: Composition, Architecture, and Transport Mechanism Rout, Michael P. Aitchison, John D. Suprapto, Adisetyantari Hjertaas, Kelly Zhao, Yingming Chait, Brian T. J Cell Biol Original Article 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. The Rockefeller University Press 2000-02-21 /pmc/articles/PMC2169373/ /pubmed/10684247 Text en © 2000 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Original Article
Rout, Michael P.
Aitchison, John D.
Suprapto, Adisetyantari
Hjertaas, Kelly
Zhao, Yingming
Chait, Brian T.
The Yeast Nuclear Pore Complex: Composition, Architecture, and Transport Mechanism
title The Yeast Nuclear Pore Complex: Composition, Architecture, and Transport Mechanism
title_full The Yeast Nuclear Pore Complex: Composition, Architecture, and Transport Mechanism
title_fullStr The Yeast Nuclear Pore Complex: Composition, Architecture, and Transport Mechanism
title_full_unstemmed The Yeast Nuclear Pore Complex: Composition, Architecture, and Transport Mechanism
title_short The Yeast Nuclear Pore Complex: Composition, Architecture, and Transport Mechanism
title_sort yeast nuclear pore complex: composition, architecture, and transport mechanism
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2169373/
https://www.ncbi.nlm.nih.gov/pubmed/10684247
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