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Emerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin–BAF Interaction and BAF Nuclear Localization
Reactive Oxygen Species (ROS) are reactive molecules required for the maintenance of physiological functions. Oxidative stress arises when ROS production exceeds the cellular ability to eliminate such molecules. In this study, we showed that oxidative stress induces post-translational modification o...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7349582/ https://www.ncbi.nlm.nih.gov/pubmed/32517247 http://dx.doi.org/10.3390/cells9061415 |
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author | Cenni, Vittoria Squarzoni, Stefano Loi, Manuela Mattioli, Elisabetta Lattanzi, Giovanna Capanni, Cristina |
author_facet | Cenni, Vittoria Squarzoni, Stefano Loi, Manuela Mattioli, Elisabetta Lattanzi, Giovanna Capanni, Cristina |
author_sort | Cenni, Vittoria |
collection | PubMed |
description | Reactive Oxygen Species (ROS) are reactive molecules required for the maintenance of physiological functions. Oxidative stress arises when ROS production exceeds the cellular ability to eliminate such molecules. In this study, we showed that oxidative stress induces post-translational modification of the inner nuclear membrane protein emerin. In particular, emerin is phosphorylated at the early stages of the oxidative stress response, while protein phosphorylation is abolished upon recovery from stress. A finely tuned balance between emerin phosphorylation and O-GlcNAcylation seems to govern this dynamic and modulates emerin–BAF interaction and BAF nucleoplasmic localization during the oxidative stress response. Interestingly, emerin post-translational modifications, similar to those observed during the stress response, are detected in cells bearing LMNA gene mutations and are characterized by a free radical generating environment. On the other hand, under oxidative stress conditions, a delay in DNA damage repair and cell cycle progression is found in cells from Emery–Dreifuss Muscular Dystrophy type 1, which do not express emerin. These results suggest a role of the emerin–BAF protein platform in the DNA damage response aimed at counteracting the detrimental effects of elevated levels of ROS. |
format | Online Article Text |
id | pubmed-7349582 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-73495822020-07-14 Emerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin–BAF Interaction and BAF Nuclear Localization Cenni, Vittoria Squarzoni, Stefano Loi, Manuela Mattioli, Elisabetta Lattanzi, Giovanna Capanni, Cristina Cells Article Reactive Oxygen Species (ROS) are reactive molecules required for the maintenance of physiological functions. Oxidative stress arises when ROS production exceeds the cellular ability to eliminate such molecules. In this study, we showed that oxidative stress induces post-translational modification of the inner nuclear membrane protein emerin. In particular, emerin is phosphorylated at the early stages of the oxidative stress response, while protein phosphorylation is abolished upon recovery from stress. A finely tuned balance between emerin phosphorylation and O-GlcNAcylation seems to govern this dynamic and modulates emerin–BAF interaction and BAF nucleoplasmic localization during the oxidative stress response. Interestingly, emerin post-translational modifications, similar to those observed during the stress response, are detected in cells bearing LMNA gene mutations and are characterized by a free radical generating environment. On the other hand, under oxidative stress conditions, a delay in DNA damage repair and cell cycle progression is found in cells from Emery–Dreifuss Muscular Dystrophy type 1, which do not express emerin. These results suggest a role of the emerin–BAF protein platform in the DNA damage response aimed at counteracting the detrimental effects of elevated levels of ROS. MDPI 2020-06-06 /pmc/articles/PMC7349582/ /pubmed/32517247 http://dx.doi.org/10.3390/cells9061415 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Cenni, Vittoria Squarzoni, Stefano Loi, Manuela Mattioli, Elisabetta Lattanzi, Giovanna Capanni, Cristina Emerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin–BAF Interaction and BAF Nuclear Localization |
title | Emerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin–BAF Interaction and BAF Nuclear Localization |
title_full | Emerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin–BAF Interaction and BAF Nuclear Localization |
title_fullStr | Emerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin–BAF Interaction and BAF Nuclear Localization |
title_full_unstemmed | Emerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin–BAF Interaction and BAF Nuclear Localization |
title_short | Emerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin–BAF Interaction and BAF Nuclear Localization |
title_sort | emerin phosphorylation during the early phase of the oxidative stress response influences emerin–baf interaction and baf nuclear localization |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7349582/ https://www.ncbi.nlm.nih.gov/pubmed/32517247 http://dx.doi.org/10.3390/cells9061415 |
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