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Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex

Unraveling the organization of the FG repeat meshwork that forms the active transport channel of the nuclear pore complex (NPC) is key to understanding the mechanism of nucleocytoplasmic transport. In this paper, we develop a tool to probe the FG repeat network in living cells by modifying FG nucleo...

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Detalles Bibliográficos
Autores principales: Stelter, Philipp, Kunze, Ruth, Fischer, Jessica, Hurt, Ed
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3198172/
https://www.ncbi.nlm.nih.gov/pubmed/21987633
http://dx.doi.org/10.1083/jcb.201105042
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author Stelter, Philipp
Kunze, Ruth
Fischer, Jessica
Hurt, Ed
author_facet Stelter, Philipp
Kunze, Ruth
Fischer, Jessica
Hurt, Ed
author_sort Stelter, Philipp
collection PubMed
description Unraveling the organization of the FG repeat meshwork that forms the active transport channel of the nuclear pore complex (NPC) is key to understanding the mechanism of nucleocytoplasmic transport. In this paper, we develop a tool to probe the FG repeat network in living cells by modifying FG nucleoporins (Nups) with a binding motif (engineered dynein light chain–interacting domain) that can drag several copies of an interfering protein, Dyn2, into the FG network to plug the pore and stop nucleocytoplasmic transport. Our method allows us to specifically probe FG Nups in vivo, which provides insight into the organization and function of the NPC transport channel.
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spelling pubmed-31981722012-04-17 Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex Stelter, Philipp Kunze, Ruth Fischer, Jessica Hurt, Ed J Cell Biol Research Articles Unraveling the organization of the FG repeat meshwork that forms the active transport channel of the nuclear pore complex (NPC) is key to understanding the mechanism of nucleocytoplasmic transport. In this paper, we develop a tool to probe the FG repeat network in living cells by modifying FG nucleoporins (Nups) with a binding motif (engineered dynein light chain–interacting domain) that can drag several copies of an interfering protein, Dyn2, into the FG network to plug the pore and stop nucleocytoplasmic transport. Our method allows us to specifically probe FG Nups in vivo, which provides insight into the organization and function of the NPC transport channel. The Rockefeller University Press 2011-10-17 /pmc/articles/PMC3198172/ /pubmed/21987633 http://dx.doi.org/10.1083/jcb.201105042 Text en © 2011 Stelter et al. 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 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
Stelter, Philipp
Kunze, Ruth
Fischer, Jessica
Hurt, Ed
Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex
title Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex
title_full Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex
title_fullStr Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex
title_full_unstemmed Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex
title_short Probing the nucleoporin FG repeat network defines structural and functional features of the nuclear pore complex
title_sort probing the nucleoporin fg repeat network defines structural and functional features of the nuclear pore complex
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3198172/
https://www.ncbi.nlm.nih.gov/pubmed/21987633
http://dx.doi.org/10.1083/jcb.201105042
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