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Lookup NU author(s): Professor Tiago OuteiroORCiD
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© 2024 Elsevier Inc.SUMOylation is a post-translational modification essential for various biological processes. SUMO proteins bind to target substrates in a three-step enzymatic pathway, which is rapidly reversible by the action of specific proteases, known as SENPs. Studies have shown that SUMOylation is dysregulated in several human disorders, including neurodegenerative diseases that are characterized by the progressive loss of neurons, mitochondrial dysfunction, deficits in autophagy, and oxidative stress. Considering the potential neuroprotective roles of SUMOylation, the aim of this study was to investigate the effects of SENP3 knockdown in H4 neuroglioma cells exposed to rotenone, an in vitro model of cytotoxicity that mimics dopaminergic loss in Parkinson's disease (PD). The current data show that SENP3 knockdown increases SUMO-2/3 conjugates, which is accompanied by reduced levels of the mitochondrial fission protein Drp1 and increased levels of the mitochondrial fusion protein OPA1. Of high interest, SENP3 knockdown prevented rotenone-induced superoxide production and cellular death. Taken together, these findings highlight the importance of SUMOylation in maintaining mitochondrial homeostasis and the neuroprotective potential of this modification in PD.
Author(s): Soares ES, Queiroz LY, Gerhardt E, Prediger RDS, Outeiro TF, Cimarosti HI
Publication type: Article
Publication status: Published
Journal: Molecular and Cellular Neuroscience
Year: 2024
Volume: 131
Online publication date: 10/09/2024
Acceptance date: 04/09/2024
ISSN (print): 1044-7431
ISSN (electronic): 1095-9327
Publisher: Elsevier
URL: https://doi.org/10.1016/j.mcn.2024.103969
DOI: 10.1016/j.mcn.2024.103969
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