The function of α-synuclein
Open accessAbstract
Human genetics has indicated a causal role for the protein α-synuclein in the pathogenesis of familial Parkinson's disease (PD), and the aggregation of synuclein in essentially all patients with PD suggests a central role for this protein in the sporadic disorder. Indeed, the accumulation of misfolded α-synuclein now defines multiple forms of neural degeneration. Like many of the proteins that accumulate in other neurodegenerative disorders, however, the normal function of synuclein remains poorly understood. In this article, we review the role of synuclein at the nerve terminal and in membrane remodeling. We also consider the prion-like propagation of misfolded synuclein as a mechanism for the spread of degeneration through the neuraxis.
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α-synuclein is derived from 140 amino acids and is made of three main groups: a highly conserved N-terminal, a hydrophobic non-amyloid β compound, and an unstructured C-terminus.
“Derived from 140 amino acids, α-syn is made of three main groups: a highly conserved N-terminal, a hydrophobic non-amyloid β compound, and an unstructured C-terminus [129].”
From The Impact of Neurotoxin Proteins Trafficked by Primary Cilia and Extracellular Vesicles in Neurodegenerative Diseases (2025) · cites this paper as [129]
The Abstract identifies α-synuclein as a 140-amino-acid protein, and “The Structure of Synuclein” describes its highly conserved N-terminal repeats and a distinct, polar C-terminus. Our copy does not describe a hydrophobic non-amyloid β component as one of three main regions, or characterize the C-terminus specifically as unstructured. (LLM, conf=0.86)
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Mice lacking alpha-synuclein are resistant to mitochondrial toxins
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Lewy Body Pathology in Normal Elderly Subjects
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Olfactory deficits in mice overexpressing human wildtype α‐synuclein
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Monomeric Synucleins Generate Membrane Curvature
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Genetic Variants of the α-Synuclein Gene SNCA Are Associated with Multiple System Atrophy
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A Combinatorial Code for the Interaction of α-Synuclein with Membranes
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Danna, R., Kondle, S., Amar, O., Mabourakh, M., Chen, G., Fadol, W. B., & Mohieldin, A. M. (2025) · Biology · doi:10.3390/biology14121787 · Cited by 2 · see citing works
“Derived from 140 amino acids, α -syn is made of three main groups: a highly conserved N-terminal, a hydrophobic non-amyloid β compound, and an unstructured C-terminus [129].”
- Authors
- Bendor, J. T., Logan, T. P., & Edwards, R. H.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Edwards, Robert H.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 79
- Issue
- 6
- Pages
- 1044-1066
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC3866954
- OpenAlex
- W2087482196
- Cited by
- 825
- References
- 318
- Citations by year
- 2026: 36 · 2025: 57 · 2024: 88 · 2023: 61 · 2022: 105 · 2021: 77 · 2020: 85 · 2019: 58 · 2018: 70 · 2017: 61 · 2016: 48 · 2015: 47 · 2014: 28 · 2013: 4
- FWCI
- 26.87
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (NS062715, R01NS062715)
- Topics
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- alpha-synuclein, Parkinson's disease, protein aggregation, synucleinopathies, membrane remodeling, prion-like propagation, neurodegeneration, familial Parkinson's disease, sporadic Parkinson's disease
- MeSH terms
- Animals, Humans, Parkinson Disease, Prions, Neurodegenerative Diseases, alpha-Synuclein
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