ArticleJournal of molecular neuroscience : MN2011
Aggregation of α-synuclein in S. cerevisiae is associated with defects in endosomal trafficking and phospholipid biosynthesis.
Article in Journal of molecular neuroscience : MN, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 70 citations in OpenAlex.
- Pathogenic mechanism underlying parkinsonism induced by neurotoxicants (MPTP and 6-hydroxydopamine) and α-synuclein: a unifying hypothesis.Journal of molecular cell biology · 2025Review
- Lipids and α-Synuclein: adding further variables to the equation.Frontiers in molecular biosciences · 2024Review
- Multiple tethers of organelle contact sites are involved in α-synuclein toxicity in yeast.Molecular biology of the cell · 2023Article
- Overexpression of alpha synuclein disrupts APP and Endolysosomal axonal trafficking in a mouse model of synucleinopathy.Neurobiology of disease · 2023Article
- Huntingtin and Other Neurodegeneration-Associated Proteins in the Development of Intracellular Pathologies: Potential Target Search for Therapeutic Intervention.International journal of molecular sciences · 2022Review
- Retrograde Axonal Autophagy and Endocytic Pathways Are Parallel and Separate in Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- α-synuclein and phosphoinositide-binding proteins: α-synuclein inhibits the association of PX- but not FYVE-containing proteins with vesicles in vivo.Biochemical and biophysical research communications · 2022Article
- A novel yeast-based screening system for potential compounds that can alleviate human α-synuclein toxicity.Journal of applied microbiology · 2022Article
- Brain regions susceptible to alpha-synuclein spreading.Molecular psychiatry · 2022Review
- Alpha-Synuclein and the Endolysosomal System in Parkinson's Disease: Guilty by Association.Biomolecules · 2021Review
- Vesicle trafficking and lipid metabolism in synucleinopathy.Acta neuropathologica · 2021Review
- Reverse engineering Lewy bodies: how far have we come and how far can we go?Nature reviews. Neuroscience · 2021Review
- An Emerging Role for Phosphoinositides in the Pathophysiology of Parkinson's Disease.Journal of Parkinson's disease · 2021Review
- Decreased Vacuolar CaFrontiers in genetics · 2020Article
- The physiological role of α-synuclein and its relationship to Parkinson's Disease.Journal of neurochemistry · 2019Review
- Probing the Origin of the Toxicity of Oligomeric Aggregates of α-Synuclein with Antibodies.ACS chemical biology · 2019Article
- The Role of Lipids in Parkinson's Disease.Cells · 2019Review
- From Yeast to Humans: Leveraging New Approaches in Yeast to Accelerate Discovery of Therapeutic Targets for Synucleinopathies.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Alpha-Synuclein Physiology and Pathology: A Perspective on Cellular Structures and Organelles.Frontiers in neuroscience · 2019Review
- Cell Biology and Pathophysiology of α-Synuclein.Cold Spring Harbor perspectives in medicine · 2018Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Parkinson's disease is the most common neurodegenerative movement disorder. α-Synuclein is a small synaptic protein that has been linked to familial Parkinson's disease (PD) and is also the primary component of Lewy bodies, the hallmark neuropathology found in the brain of sporadic and familial PD patients. The function of α-synuclein is currently unknown, although it has been implicated in the regulation of synaptic vesicle localization or fusion. Recently, overexpression of α-synuclein was shown to cause cytoplasmic vesicle accumulation in a yeast model of α-synuclein toxicity, but the exact role α-synuclein played in mediating this vesicle aggregation is unclear. Here, we show that α-synuclein induces aggregation of many yeast Rab GTPase proteins, that α-synuclein aggregation is enhanced in yeast mutants that produce high levels of acidic phospholipids, and that α-synuclein colocalizes with yeast membranes that are enriched for phosphatidic acid. Significantly, we demonstrate that α-synuclein expression induces vulnerability to perturbations of Ypt6 and other proteins involved in retrograde endosome-Golgi transport, linking a specific trafficking defect to α-synuclein phospholipid binding. These data suggest new pathogenic mechanisms for α-synuclein neurotoxicity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.