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Emerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin–BAF Interaction and BAF Nuclear Localization

1
CNR Institute of Molecular Genetics “Luigi Luca Cavalli-Sforza”, Unit of Bologna, 40136 Bologna, Italy
2
IRCCS Istituto Ortopedico Rizzoli, 40136 Bologna, Italy
3
Department of Biomedical and Neuromotor Sciences, University of Bologna, 40127 Bologna, Italy
*
Author to whom correspondence should be addressed.
Cells 2020, 9(6), 1415; https://doi.org/10.3390/cells9061415
Received: 19 May 2020 / Revised: 4 June 2020 / Accepted: 4 June 2020 / Published: 6 June 2020
(This article belongs to the Section Cell Nuclei: Function, Transport and Receptors)
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. View Full-Text
Keywords: emerin; EDMD1; BAF; BANF1; laminA/C; laminopathies; chromatin; prelamin A; DNA-damage response; oxidative stress emerin; EDMD1; BAF; BANF1; laminA/C; laminopathies; chromatin; prelamin A; DNA-damage response; oxidative stress
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Cenni, V.; Squarzoni, S.; Loi, M.; Mattioli, E.; Lattanzi, G.; Capanni, C. Emerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin–BAF Interaction and BAF Nuclear Localization. Cells 2020, 9, 1415.

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