ArticleNPJ Parkinson's disease2019
Regulation of exocytosis and mitochondrial relocalization by Alpha-synuclein in a mammalian cell model.
Article in NPJ Parkinson's disease, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- α-Synuclein aggregation landscape from phase separation to neurotoxic intermediates.FEBS letters · 2026Review
- Alpha-synuclein modulates the positioning of endolysosomes in melanoma cells.Human molecular genetics · 2025Article
- Plasma acellular transcriptome contains Parkinson's disease signatures that can inform clinical diagnosis.medRxiv : the preprint server for health sciences · 2024Article
- Pulsed electric field induces exocytosis and overexpression of MAGE antigens in melanoma.Scientific reports · 2024Article
- The Effects of Lipids on α-Synuclein Aggregation In Vitro.Biomolecules · 2023Review
- Alpha synuclein modulates mitochondrial CaNPJ Parkinson's disease · 2023Article
- Exploring Intra- and Inter-Regional Interactions in the IDP α-Synuclein Using smFRET and MD Simulations.Biomacromolecules · 2023Article
- α-Synuclein and biological membranes: the danger of loving too much.Chemical communications (Cambridge, England) · 2023Review
- Alpha Synuclein Modulates Mitochondrial CabioRxiv : the preprint server for biology · 2023Article
- Quantitative Seed Amplification Assay: A Proof-of-Principle Study.The journal of physical chemistry. B · 2023Article
- The Role of Membrane Affinity and Binding Modes in Alpha-Synuclein Regulation of Vesicle Release and Trafficking.Biomolecules · 2022Article
- Interactions between SARS-CoV-2 N-Protein and α-Synuclein Accelerate Amyloid Formation.ACS chemical neuroscience · 2022Article
- Plasticity of Membrane Binding by the Central Region of α-Synuclein.Frontiers in molecular biosciences · 2022Article
- α-Synuclein kinetically regulates the nascent fusion pore dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition.Nature communications · 2021Article
- Megadalton-sized Dityrosine Aggregates of α-Synuclein Retain High Degrees of Structural Disorder and Internal Dynamics.Journal of molecular biology · 2020Article
- Dynamic instability of clathrin assembly provides proofreading control for endocytosis.The Journal of cell biology · 2019Article
- Membrane interactions of intrinsically disordered proteins: The example of alpha-synuclein.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- Intrinsically disordered proteins in synaptic vesicle trafficking and release.The Journal of biological chemistry · 2019Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
We characterized phenotypes in RBL-2H3 mast cells transfected with human alpha synuclein (a-syn) using stimulated exocytosis of recycling endosomes as a proxy for similar activities of synaptic vesicles in neurons. We found that low expression of a-syn inhibits stimulated exocytosis and that higher expression causes slight enhancement. NMR measurements of membrane interactions correlate with these functional effects: they are eliminated differentially by mutants that perturb helical structure in the helix 1 (A30P) or NAC/helix-2 (V70P) regions of membrane-bound a-syn, but not by other PD-associated mutants or C-terminal truncation. We further found that a-syn (but not A30P or V70P mutants) associates weakly with mitochondria, but this association increases markedly under conditions of cellular stress. These results highlight the importance of specific structural features of a-syn in regulating vesicle release, and point to a potential role for a-syn in perturbing mitochondrial function under pathological conditions.
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