ArticleThe Journal of biological chemistry2013
α-Synuclein oligomers with broken helical conformation form lipoprotein nanoparticles.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Peripheral membrane protein endophilin B1 probes, perturbs and permeabilizes lipid bilayers.Communications biology · 2025Article
- The inhibitory action of the chaperone BRICHOS against the α-Synuclein secondary nucleation pathway.Nature communications · 2024Article
- A Relationship between the Structures and Neurotoxic Effects of Aβ Oligomers Stabilized by Different Metal Ions.ACS chemical neuroscience · 2024Article
- High-resolution structural information of membrane-bound α-synuclein provides insight into the MoA of the anti-Parkinson drug UCB0599.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Review
- Generation of nanoscopic membrane curvature for membrane trafficking.Nature reviews. Molecular cell biology · 2023Review
- Sorting Out Sorting Nexins Functions in the Nervous System in Health and Disease.Molecular neurobiology · 2021Review
- Mechanism of membrane-curvature generation by ER-tubule shaping proteins.Nature communications · 2021Article
- Membrane Interactions of α-Synuclein Probed by Neutrons and Photons.Accounts of chemical research · 2021Article
- Rapid Formation of Peptide/Lipid Coaggregates by the Amyloidogenic Seminal Peptide PAPBiophysical journal · 2020Article
- Unroofing site-specific α-synuclein-lipid interactions at the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cholesterol Metabolism in the Brain and Its Association with Parkinson's Disease.Experimental neurobiology · 2019Review
- Structure of Membrane-Bound Huntingtin Exon 1 Reveals Membrane Interaction and Aggregation Mechanisms.Structure (London, England : 1993) · 2019Article
- Lipid and immune abnormalities causing age-dependent neurodegeneration and Parkinson's disease.Journal of neuroinflammation · 2019Review
- E46K-like α-synuclein mutants increase lipid interactions and disrupt membrane selectivity.The Journal of biological chemistry · 2019Article
- α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation.Chemistry and physics of lipids · 2019Article
- Interplay between α-synuclein amyloid formation and membrane structure.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- Novel Results and Concepts Emerging From Lipid Cell Biology Relevant to Degenerative Brain Aging and Disease.Frontiers in neurology · 2019Review
- Membranes as modulators of amyloid protein misfolding and target of toxicity.Biochimica et biophysica acta. Biomembranes · 2018Review
- Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules.Biochimica et biophysica acta. Biomembranes · 2018Article
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Authors and funding
6 authors.
Funding
Abstract
α-Synuclein (αS) is a membrane-binding protein with sequence similarity to apolipoproteins and other lipid-carrying proteins, which are capable of forming lipid-containing nanoparticles, sometimes referred to as "discs." Previously, it has been unclear whether αS also possesses this property. Using cryo-electron microscopy and light scattering, we found that αS can remodel phosphatidylglycerol vesicles into nanoparticles whose shape (ellipsoidal) and dimensions (in the 7-10-nm range) resemble those formed by apolipoproteins. The molar ratio of αS to lipid in nanoparticles is ∼1:20, and αS is oligomeric (including trimers and tetramers). Similar nanoparticles form when αS is added to vesicles of mitochondrial lipids. This observation suggests a mechanism for the previously reported disruption of mitochondrial membranes by αS. Circular dichroism and four-pulse double electron electron resonance experiments revealed that in nanoparticles αS assumes a broken helical conformation distinct from the extended helical conformation adopted when αS is bound to intact vesicles or membrane tubules. We also observed αS-dependent tubule and nanoparticle formation in the presence of oleic acid, implying that αS can interact with fatty acids and lipids in a similar manner. αS-related nanoparticles might play a role in lipid and fatty acid transport functions previously attributed to this protein.
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