SIRT3-Mediated Deacetylation of DRP1^K711 Prevents Mitochondrial Dysfunction in Parkinson's Disease.

ABSTRACT: Dysregulation of mitochondrial dynamics is a key contributor to the pathogenesis of Parkinson's disease (PD). Aberrant mitochondrial fission induced by dynamin-related protein 1 (DRP1) causes mitochondrial dysfunction in dopaminergic (DA) neurons. However, the mechanism of DRP1 activation and its role in PD progression remain unclear. In this study, Mass spectrometry analysis is performed and identified a significant increased DRP1 acetylation at lysine residue 711 (K711) in the mitochondria under oxidative stress. Enhanced DRP1^K711 acetylation facilitated DRP1 oligomerization, thereby exacerbating mitochondrial fragmentation and compromising the mitochondrial function. DRP1^K711 acetylation also affects mitochondrial DRP1 recruitment and fission independent of canonic

SUBMITTER: Xi Y 

PROVIDER: S-EPMC12061286 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature