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

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1415
Author(s):  
Vittoria Cenni ◽  
Stefano Squarzoni ◽  
Manuela Loi ◽  
Elisabetta Mattioli ◽  
Giovanna Lattanzi ◽  
...  

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.

2014 ◽  
Vol 26 (6) ◽  
pp. 825-829 ◽  
Author(s):  
Xing-Yu Huang ◽  
Wichai Eungpinichpong ◽  
Atit Silsirivanit ◽  
Saowanee Nakmareong ◽  
Xiu-Hua Wu

Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 1089-1089
Author(s):  
Jie Li ◽  
Suzette Maynard ◽  
Paul R. Andreassen ◽  
Qishen Pang

Abstract Abstract 1089 Poster Board I-111 Fanconi anemia (FA) is a human genomic instability syndrome that is uniquely sensitive to oxidative stress. Members of the FA protein family are involved in repair of genetic damage caused by DNA cross-linkers. The molecular pathway in which the FA proteins function in oxidative stress response has not been defined. Here we report functional interaction between the FA protein FANCD2 and the forkhead transcription factor FOXO3a in response to oxidative stress. FOXO3a was colocalized to FANCD2 foci in cells subjected to oxidative stress. The FANCD2-FOXO3a complex was not detected in cells deficient for the FA core complex component FANCA, but could be restored after complementation with a functional FANCA. Consistent with this, a non-monoubiquitinated FANCD2 mutant failed to bind FOXO3a. While both DNA cross-linker mitomycin C and ionizing radiation induced monoubiquitination of FANCD2, neither was able to induce the association of FANCD2 and FOXO3a. This indicates that the FOXO3a-FANCD2 interaction is oxidative stress specific. Overexpression of FOXO3a reduced abnormal accumulation of reactive oxygen species, enhanced cellular resistance to oxidative stress, and increased antioxidant gene expression in corrected but not mutant FA-D2 cells. The novel oxidative stress response pathway converging FANCD2 and FOXO3a identified in this study is likely to contribute to cellular anti-oxidant defense. Disclosures No relevant conflicts of interest to declare.


Nanoscale ◽  
2017 ◽  
Vol 9 (22) ◽  
pp. 7595-7601 ◽  
Author(s):  
Dhanya T. Jayaram ◽  
Sabiha Runa ◽  
Melissa L. Kemp ◽  
Christine K. Payne

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