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Cited by 619Parkinson's Disease Mechanisms and TreatmentsMitochondrial Function and PathologyNuclear Receptors and Signaling

α-Synuclein binds to TOM20 and inhibits mitochondrial protein import in Parkinson’s disease

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Di Maio, Roberto, Barrett, Paul J., Hoffman, Eric K., Barrett, Caitlyn W., Zharikov, Alevtina, Borah, Anupom, Hu, Xiaoping, McCoy, Jennifer +4 more·2016·Science Translational Medicine
DOI 10.1126/scitranslmed.aaf3634PMC PMC5016095
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Abstract

The Parkinson’s disease–associated protein α-synuclein binds to the mitochondrial protein import receptor TOM20, which causes downstream impairment of mitochondrial function.

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Crossref · 10.1126/scitranslmed.aaf3634

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  • Other in vitro studies revealed oligomeric α-synuclein induced mitochondrial dysfunction and neuronal death through multiple mechanisms.

    “But other in vitro studies revealed that oligomeric α-synuclein induced mitochondrial dysfunction and neuronal death through multiple mechanisms.56,57”

    From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [57]

    The Results sections on α-synuclein import and downstream consequences report that oligomeric α-synuclein impaired mitochondrial protein import in vitro, reduced respiration, and caused oxidative damage and mitochondrial depolarization. The Discussion describes these as consequences of protein-import impairment but says its contribution to overall neurotoxicity remains undetermined. The paper does not establish neuronal death or multiple mechanisms causing it. (LLM, conf=0.87)

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Research works printed but not linked: 44

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Cited by

Sorted by citations

Authors
Di Maio, R., Barrett, P. J., Hoffman, E. K., Barrett, C. W., Zharikov, A., Borah, A., Hu, X., McCoy, J., Chu, C. T., Burton, E. A., Hastings, T. G., & Greenamyre, J. T.
Affiliations
  • Pittsburgh Institute for Neurodegenerative Diseases, University of Pittsburgh, Pittsburgh, PA 15213, USA.
  • University of Pittsburgh (US)
Corresponding author
  • Barrett, Paul J.
  • Greenamyre, J. Timothy
ORCID
Venue
Science Translational Medicine
Publisher
American Association for the Advancement of Science (AAAS)
Published
2016-06-08
Volume
8
Issue
342
Pages
342ra78-342ra78
ISSN
  • 1946-6234 (ISSN-L)
  • 1946-6242
DOI
10.1126/scitranslmed.aaf3634
PMC
PMC5016095
OpenAlex
W2417395660
Cited by
619
References
3
Citations by year
2026: 48 · 2025: 59 · 2024: 58 · 2023: 82 · 2022: 59 · 2021: 75 · 2020: 64 · 2019: 58 · 2018: 54 · 2017: 52 · 2016: 10
FWCI
43.62
Type
journal article
Language
en
Open access
Licence
www.sciencemag.org/about/science-licenses-journal-article-reuse (vor, 365 d)
Locations
  • Science Translational Medicine (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • DSF Charitable Foundation
  • Ri.MED Foundation
  • Consolidated Anti-Aging Foundation
  • NIH (NS095387, NS059806, ES022644, ES020718, ES020327, NS065789, AG026389, P50AG005133)
  • U.S. Department of Veterans Affairs (1I01BX000548)
  • Blechman Foundation
  • American Parkinson Disease Association
  • Department of Biotechnology, Government of India
Topics
  • Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
Keywords
alpha-synuclein, Tom20, Tom22, mitochondrial protein import, Parkinson's disease, mitochondrial dysfunction, reactive oxygen species, mitochondrial membrane potential, mitochondrial respiration, nigrostriatal dopaminergic neurons, neuroprotection
MeSH terms
Mitochondrial Precursor Protein Import Complex Proteins, Animals, Mitochondria, Parkinson Disease, Protein Binding, Rats, Mutant Strains, Receptors, Cell Surface, Receptors, Cytoplasmic and Nuclear, Protein Transport, Mitochondrial Proteins, Membrane Transport Proteins, Rats, alpha-Synuclein

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