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ESCRTs breach the nuclear border

The endosomal sorting complexes required for transport (ESCRT) are best known for their role in sorting ubiquitylated membrane proteins into endosomes. The most ancient component of the ESCRT machinery is ESCRT-III, which is capable of oligomerizing into a helical filament that drives the invaginati...

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Autores principales: Webster, Brant M, Lusk, C Patrick
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4615171/
https://www.ncbi.nlm.nih.gov/pubmed/25942571
http://dx.doi.org/10.1080/19491034.2015.1035844
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author Webster, Brant M
Lusk, C Patrick
author_facet Webster, Brant M
Lusk, C Patrick
author_sort Webster, Brant M
collection PubMed
description The endosomal sorting complexes required for transport (ESCRT) are best known for their role in sorting ubiquitylated membrane proteins into endosomes. The most ancient component of the ESCRT machinery is ESCRT-III, which is capable of oligomerizing into a helical filament that drives the invagination and scission of membranes aided by the AAA ATPase, Vps4, in several additional subcellular contexts. Our recent study broadens the work of ESCRT-III by identifying its role in a quality control pathway at the nuclear envelope (NE) that ensures the normal biogenesis of nuclear pore complexes (NPCs). Here, we will elaborate on how we envision this mechanism to progress and incorporate ESCRT-III into an emerging model of nuclear pore formation. Moreover, we speculate there are additional roles for the ESCRT-III machinery at the NE that broadly function to ensure its integrity and the maintenance of the nuclear compartment.
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spelling pubmed-46151712016-02-03 ESCRTs breach the nuclear border Webster, Brant M Lusk, C Patrick Nucleus Extra View The endosomal sorting complexes required for transport (ESCRT) are best known for their role in sorting ubiquitylated membrane proteins into endosomes. The most ancient component of the ESCRT machinery is ESCRT-III, which is capable of oligomerizing into a helical filament that drives the invagination and scission of membranes aided by the AAA ATPase, Vps4, in several additional subcellular contexts. Our recent study broadens the work of ESCRT-III by identifying its role in a quality control pathway at the nuclear envelope (NE) that ensures the normal biogenesis of nuclear pore complexes (NPCs). Here, we will elaborate on how we envision this mechanism to progress and incorporate ESCRT-III into an emerging model of nuclear pore formation. Moreover, we speculate there are additional roles for the ESCRT-III machinery at the NE that broadly function to ensure its integrity and the maintenance of the nuclear compartment. Taylor & Francis 2015-05-05 /pmc/articles/PMC4615171/ /pubmed/25942571 http://dx.doi.org/10.1080/19491034.2015.1035844 Text en © 2015 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License http://creativecommons.org/licenses/by-nc/3.0/, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
spellingShingle Extra View
Webster, Brant M
Lusk, C Patrick
ESCRTs breach the nuclear border
title ESCRTs breach the nuclear border
title_full ESCRTs breach the nuclear border
title_fullStr ESCRTs breach the nuclear border
title_full_unstemmed ESCRTs breach the nuclear border
title_short ESCRTs breach the nuclear border
title_sort escrts breach the nuclear border
topic Extra View
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4615171/
https://www.ncbi.nlm.nih.gov/pubmed/25942571
http://dx.doi.org/10.1080/19491034.2015.1035844
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