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Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution
The biogenesis of nuclear pore complexes (NPCs) represents a paradigm for the assembly of high-complexity macromolecular structures. So far, only three integral pore membrane proteins are known to function redundantly in NPC anchoring within the nuclear envelope. Here, we describe the identification...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2878943/ https://www.ncbi.nlm.nih.gov/pubmed/20498018 http://dx.doi.org/10.1083/jcb.200910043 |
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author | Chadrin, Anne Hess, Barbara San Roman, Mabel Gatti, Xavier Lombard, Bérangère Loew, Damarys Barral, Yves Palancade, Benoit Doye, Valérie |
author_facet | Chadrin, Anne Hess, Barbara San Roman, Mabel Gatti, Xavier Lombard, Bérangère Loew, Damarys Barral, Yves Palancade, Benoit Doye, Valérie |
author_sort | Chadrin, Anne |
collection | PubMed |
description | The biogenesis of nuclear pore complexes (NPCs) represents a paradigm for the assembly of high-complexity macromolecular structures. So far, only three integral pore membrane proteins are known to function redundantly in NPC anchoring within the nuclear envelope. Here, we describe the identification and functional characterization of Pom33, a novel transmembrane protein dynamically associated with budding yeast NPCs. Pom33 becomes critical for yeast viability in the absence of a functional Nup84 complex or Ndc1 interaction network, which are two core NPC subcomplexes, and associates with the reticulon Rtn1. Moreover, POM33 loss of function impairs NPC distribution, a readout for a subset of genes required for pore biogenesis, including members of the Nup84 complex and RTN1. Consistently, we show that Pom33 is required for normal NPC density in the daughter nucleus and for proper NPC biogenesis and/or stability in the absence of Nup170. We hypothesize that, by modifying or stabilizing the nuclear envelope–NPC interface, Pom33 may contribute to proper distribution and/or efficient assembly of nuclear pores. |
format | Text |
id | pubmed-2878943 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-28789432010-11-30 Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution Chadrin, Anne Hess, Barbara San Roman, Mabel Gatti, Xavier Lombard, Bérangère Loew, Damarys Barral, Yves Palancade, Benoit Doye, Valérie J Cell Biol Research Articles The biogenesis of nuclear pore complexes (NPCs) represents a paradigm for the assembly of high-complexity macromolecular structures. So far, only three integral pore membrane proteins are known to function redundantly in NPC anchoring within the nuclear envelope. Here, we describe the identification and functional characterization of Pom33, a novel transmembrane protein dynamically associated with budding yeast NPCs. Pom33 becomes critical for yeast viability in the absence of a functional Nup84 complex or Ndc1 interaction network, which are two core NPC subcomplexes, and associates with the reticulon Rtn1. Moreover, POM33 loss of function impairs NPC distribution, a readout for a subset of genes required for pore biogenesis, including members of the Nup84 complex and RTN1. Consistently, we show that Pom33 is required for normal NPC density in the daughter nucleus and for proper NPC biogenesis and/or stability in the absence of Nup170. We hypothesize that, by modifying or stabilizing the nuclear envelope–NPC interface, Pom33 may contribute to proper distribution and/or efficient assembly of nuclear pores. The Rockefeller University Press 2010-05-31 /pmc/articles/PMC2878943/ /pubmed/20498018 http://dx.doi.org/10.1083/jcb.200910043 Text en © 2010 Chadrin 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 Chadrin, Anne Hess, Barbara San Roman, Mabel Gatti, Xavier Lombard, Bérangère Loew, Damarys Barral, Yves Palancade, Benoit Doye, Valérie Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution |
title | Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution |
title_full | Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution |
title_fullStr | Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution |
title_full_unstemmed | Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution |
title_short | Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution |
title_sort | pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2878943/ https://www.ncbi.nlm.nih.gov/pubmed/20498018 http://dx.doi.org/10.1083/jcb.200910043 |
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