The ubiquitin pathway in Parkinson's disease

The ubiquitin pathway in Parkinson's disease

Mutations of the α-synuclein gene, have been identified in some familial forms of Parkinson's disease, and α-synuclein protein has been shown to accumulate in the brains of patients with the disease. These findings suggest that Parkinson's disease may be caused by the abnormal aggregation...

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Bibliographic Details
Published in:Nature (London) Vol. 395; no. 6701; pp. 451 - 452
Main Authors: Leroy, Elisabeth, Boyer, Rebecca, Auburger, Georg, Leube, Barbara, Ulm, Gudrun, Mezey, Eva, Harta, Gyongyi, Brownstein, Michael J, Jonnalagada, Sobhanadditya, Chernova, Tanya, Dehejia, Anindya, Lavedan, Christian, Gasser, Thomas, Steinbach, Peter J, Wilkinson, Keith D, Polymeropoulos, Mihael H
Format: Journal Article
Language:English
Published: England Nature Publishing Group 01-10-1998
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Brain - enzymology
Catalysis
DNA
Escherichia coli
Female
Humans
Male
Mice
Middle Aged
Molecular Sequence Data
Mutation
Parkinson Disease - genetics
Parkinson Disease - metabolism
Parkinson's disease
Point Mutation
Rats
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Thiolester Hydrolases - genetics
Thiolester Hydrolases - metabolism
Ubiquitin Thiolesterase
Ubiquitins - metabolism
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Summary:Mutations of the α-synuclein gene, have been identified in some familial forms of Parkinson's disease, and α-synuclein protein has been shown to accumulate in the brains of patients with the disease. These findings suggest that Parkinson's disease may be caused by the abnormal aggregation of α-synuclein protein. Here we have identified in a German family with Parkinson's disease a missense mutation in the ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) gene. We show that this mutation, Ile93Met, causes a partial loss of the catalytic activity of this thiol protease, which could lead to aberrations in the proteolytic pathway and aggregation of proteins.
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ISSN:0028-0836
1476-4687
DOI:10.1038/26652