Cited by 750Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and SignalingUbiquitin and proteasome pathways

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Parkin ubiquitinates the α-synuclein–interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease

Chung, Kenny K.K., Zhang, Yi, Lim, Kah Leong, Tanaka, Yuji, Huang, Hui, Gao, Jun, Ross, Christopher A., Dawson, Valina L., Dawson, Ted M.·2001·Nature Medicine

DOI 10.1038/nm1001-1144

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Abstract

Parkinson disease is a common neurodegenerative disorder characterized by the loss of dopaminergic neurons and the presence of intracytoplasmic-ubiquitinated inclusions (Lewy bodies). Mutations in alpha-synuclein (A53T, A30P) and parkin cause familial Parkinson disease. Both these proteins are found in Lewy bodies. The absence of Lewy bodies in patients with parkin mutations suggests that parkin might be required for the formation of Lewy bodies. Here we show that parkin interacts with and ubiquitinates the alpha-synuclein-interacting protein, synphilin-1. Co-expression of alpha-synuclein, synphilin-1 and parkin result in the formation of Lewy-body-like ubiquitin-positive cytosolic inclusions. We further show that familial-linked mutations in parkin disrupt the ubiquitination of synphilin-1 and the formation of the ubiquitin-positive inclusions. These results provide a molecular basis for the ubiquitination of Lewy-body-associated proteins and link parkin and alpha-synuclein in a common pathogenic mechanism through their interaction with synphilin-1.

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Authors: Chung, K. K. K., Zhang, Y., Lim, K. L., Tanaka, Y., Huang, H., Gao, J., Ross, C. A., Dawson, V. L., & Dawson, T. M.
Affiliations: Johns Hopkins University (US)
Corresponding author: Dawson, Ted M.
ORCID: Chung, Kenny K.K.
Zhang, Yi
Tanaka, Yuji
Huang, Hui
Dawson, Valina L.
Dawson, Ted M.
Venue: Nature Medicine
Publisher: Springer Science and Business Media LLC
Published: 2001-10
Volume: 7
Issue: 10
Pages: 1144-1150
ISSN: 1078-8956 (ISSN-L)
1546-170X
DOI: 10.1038/nm1001-1144
OpenAlex: W1529474377
Cited by: 750
References: 47
Citations by year: 2026: 10 · 2025: 11 · 2024: 15 · 2023: 22 · 2022: 11 · 2021: 23 · 2020: 18 · 2019: 12 · 2018: 14 · 2017: 21 · 2016: 22 · 2015: 20 · 2014: 17 · 2013: 17 · 2012: 27
FWCI: 42.95
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Medicine (publishedVersion)
PubMed (publishedVersion)
Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
National University of Singapore (submittedVersion)
Funders: National Institute of Neurological Disorders and Stroke (NS 38377, P50NS038377)
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: Parkin, synphilin-1, alpha-synuclein, ubiquitination, Lewy bodies, Parkinson's disease, familial Parkinson's disease, protein-protein interaction, ubiquitin-positive inclusions, parkin mutations, alpha-synuclein mutations
MeSH terms: Animals, Carrier Proteins, Cell Line, Glycosylation, Humans, Ligases, Nerve Tissue Proteins, Parkinson Disease, Ubiquitins, Mutagenesis, Lewy Bodies, Ubiquitin-Protein Ligases, Rats, Synucleins, alpha-Synuclein

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Parkin ubiquitinates the α-synuclein–interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease

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