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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...

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Autores principales: Cenni, Vittoria, Squarzoni, Stefano, Loi, Manuela, Mattioli, Elisabetta, Lattanzi, Giovanna, Capanni, Cristina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
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.
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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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