Cited by 227Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and SignalingAlzheimer's disease research and treatments

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α-synuclein Induces Mitochondrial Dysfunction through Spectrin and the Actin Cytoskeleton

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Ordonez, Dalila G., Lee, Michael K., Feany, Mel B.·2018·Neuron

DOI 10.1016/j.neuron.2017.11.036PMC PMC5755717

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Abstract

Genetics and neuropathology strongly link α-synuclein aggregation and neurotoxicity to the pathogenesis of Parkinson's disease and related α-synucleinopathies. Here we describe a new Drosophila model of α-synucleinopathy based on widespread expression of wild-type human α-synuclein, which shows robust neurodegeneration, early-onset locomotor deficits, and abundant α-synuclein aggregation. We use results of forward genetic screening and genetic analysis in our new model to demonstrate that α-synuclein expression promotes reorganization of the actin filament network and consequent mitochondrial dysfunction through altered Drp1 localization. Similar changes are present in a mouse α-synucleinopathy model and in postmortem brain tissue from patients with α-synucleinopathy. Importantly, we provide evidence that the interaction of α-synuclein with spectrin initiates pathological alteration of the actin cytoskeleton and downstream neurotoxicity. These findings suggest new therapeutic approaches for α-synuclein induced neurodegeneration.

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Authors: Ordonez, D. G., Lee, M. K., & Feany, M. B.
Affiliations: Brigham and Women's Hospital (US)
University of Minnesota (US)
ORCID: Lee, Michael K.
Venue: Neuron
Publisher: Elsevier BV
Published: 2018-01
Volume: 97
Issue: 1
Pages: 108-124.e6
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/j.neuron.2017.11.036
PMC: PMC5755717
OpenAlex: W2771082365
Cited by: 227
References: 66
Citations by year: 2026: 11 · 2025: 20 · 2024: 31 · 2023: 24 · 2022: 30 · 2021: 41 · 2020: 31 · 2019: 26 · 2018: 13
FWCI: 13.33
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 367 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
Funders: National Science Foundation (DGE1745303, DGE1144152)
National Institutes of Health (R01-NS086074, R01-NS092093, R01-AG044113, R01-NS083391)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Keywords: alpha-synuclein, Parkinson's disease, synucleinopathies, spectrin, actin cytoskeleton, mitochondrial dysfunction, Drp1, mitochondrial fission, Drosophila model, neurodegeneration, alpha-synuclein aggregation, locomotor deficits, forward genetic screen
MeSH terms: Aged, Aged, 80 and over, Animals, Cytoskeletal Proteins, Disease Models, Animal, Drosophila melanogaster, Female, Humans, Male, Actin Cytoskeleton, Middle Aged, Mitochondria, Nerve Degeneration, Spectrin, GTP-Binding Proteins, Lewy Body Disease, alpha-Synuclein

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α-synuclein Induces Mitochondrial Dysfunction through Spectrin and the Actin Cytoskeleton

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