ATP synthase nLC-MSMS - α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson's disease
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Orbitrap Fusion ETD
ORGANISM(S): Rattus Norvegicus (rat)
TISSUE(S): Brain
SUBMITTER: 
Morana Jaganjac
LAB HEAD: Morana Jaganjac
PROVIDER: PXD009416 | Pride | 2018-06-18
REPOSITORIES: Pride
Dataset's files
Publications
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson's disease.
Ludtmann Marthe H R MHR Angelova Plamena R PR Horrocks Mathew H MH Choi Minee L ML Rodrigues Margarida M Baev Artyom Y AY Berezhnov Alexey V AV Yao Zhi Z Little Daniel D Banushi Blerida B Al-Menhali Afnan Saleh AS Ranasinghe Rohan T RT Whiten Daniel R DR Yapom Ratsuda R Dolt Karamjit Singh KS Devine Michael J MJ Gissen Paul P Kunath Tilo T Jaganjac Morana M Pavlov Evgeny V EV Klenerman David D Abramov Andrey Y AY Gandhi Sonia S
Nature communications 20180612 1
Protein aggregation causes α-synuclein to switch from its physiological role to a pathological toxic gain of function. Under physiological conditions, monomeric α-synuclein improves ATP synthase efficiency. Here, we report that aggregation of monomers generates beta sheet-rich oligomers that localise to the mitochondria in close proximity to several mitochondrial proteins including ATP synthase. Oligomeric α-synuclein impairs complex I-dependent respiration. Oligomers induce selective oxidation ...[more]
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