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Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum
The nuclear envelope (NE) and endoplasmic reticulum (ER) are components of the same contiguous membrane system and yet have distinct cellular functions. Mounting evidence suggests roles for some ER proteins in the NE for proper nuclear pore complex (NPC) structure and function. In this study, we ide...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571342/ https://www.ncbi.nlm.nih.gov/pubmed/26041935 http://dx.doi.org/10.1091/mbc.E15-01-0053 |
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author | Casey, Amanda K. Chen, Shuliang Novick, Peter Ferro-Novick, Susan Wente, Susan R. |
author_facet | Casey, Amanda K. Chen, Shuliang Novick, Peter Ferro-Novick, Susan Wente, Susan R. |
author_sort | Casey, Amanda K. |
collection | PubMed |
description | The nuclear envelope (NE) and endoplasmic reticulum (ER) are components of the same contiguous membrane system and yet have distinct cellular functions. Mounting evidence suggests roles for some ER proteins in the NE for proper nuclear pore complex (NPC) structure and function. In this study, we identify a NE role in Saccharomyces cerevisiae for Lnp1 and Sey1, proteins required for proper cortical ER formation. Both lnp1Δ and sey1Δ mutants exhibit synthetic genetic interactions with mutants in genes encoding key NPC structural components. Both Lnp1 and Sey1 physically associate with other ER components that have established NPC roles, including Rtn1, Yop1, Pom33, and Per33. Of interest, lnp1Δ rtn1Δ mutants but not rtn1Δ sey1Δ mutants exhibit defects in NPC distribution. Furthermore, the essential NPC assembly factor Ndc1 has altered interactions in the absence of Sey1. Lnp1 dimerizes in vitro via its C-terminal zinc finger motif, a property that is required for proper ER structure but not NPC integrity. These findings suggest that Lnp1's role in NPC integrity is separable from functions in the ER and is linked to Ndc1 and Rtn1 interactions. |
format | Online Article Text |
id | pubmed-4571342 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-45713422015-10-16 Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum Casey, Amanda K. Chen, Shuliang Novick, Peter Ferro-Novick, Susan Wente, Susan R. Mol Biol Cell Articles The nuclear envelope (NE) and endoplasmic reticulum (ER) are components of the same contiguous membrane system and yet have distinct cellular functions. Mounting evidence suggests roles for some ER proteins in the NE for proper nuclear pore complex (NPC) structure and function. In this study, we identify a NE role in Saccharomyces cerevisiae for Lnp1 and Sey1, proteins required for proper cortical ER formation. Both lnp1Δ and sey1Δ mutants exhibit synthetic genetic interactions with mutants in genes encoding key NPC structural components. Both Lnp1 and Sey1 physically associate with other ER components that have established NPC roles, including Rtn1, Yop1, Pom33, and Per33. Of interest, lnp1Δ rtn1Δ mutants but not rtn1Δ sey1Δ mutants exhibit defects in NPC distribution. Furthermore, the essential NPC assembly factor Ndc1 has altered interactions in the absence of Sey1. Lnp1 dimerizes in vitro via its C-terminal zinc finger motif, a property that is required for proper ER structure but not NPC integrity. These findings suggest that Lnp1's role in NPC integrity is separable from functions in the ER and is linked to Ndc1 and Rtn1 interactions. The American Society for Cell Biology 2015-08-01 /pmc/articles/PMC4571342/ /pubmed/26041935 http://dx.doi.org/10.1091/mbc.E15-01-0053 Text en © 2015 Casey et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Casey, Amanda K. Chen, Shuliang Novick, Peter Ferro-Novick, Susan Wente, Susan R. Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum |
title | Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum |
title_full | Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum |
title_fullStr | Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum |
title_full_unstemmed | Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum |
title_short | Nuclear pore complex integrity requires Lnp1, a regulator of cortical endoplasmic reticulum |
title_sort | nuclear pore complex integrity requires lnp1, a regulator of cortical endoplasmic reticulum |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571342/ https://www.ncbi.nlm.nih.gov/pubmed/26041935 http://dx.doi.org/10.1091/mbc.E15-01-0053 |
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