1. α-Synuclein overexpression promotes aggregation of mutant huntingtin
- Author
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David C. Rubinsztein, Julia Rankin, Andreas Wyttenbach, Yolanda Narain, and Robert A. Furlong
- Subjects
Alpha-synuclein ,congenital, hereditary, and neonatal diseases and abnormalities ,Huntingtin ,Chemistry ,Mutant ,Cell Biology ,Transfection ,Protein aggregation ,Biochemistry ,Molecular biology ,nervous system diseases ,Green fluorescent protein ,chemistry.chemical_compound ,nervous system ,mental disorders ,Huntingtin Protein ,Nuclear protein ,Molecular Biology - Abstract
Protein aggregates are a neuropathological feature of Huntington's disease and Parkinson's disease. Mutant huntingtin exon 1 with 72 CAG repeats fused to enhanced green fluorescent protein (EGFP) forms hyperfluorescent inclusions in PC12 cells. Inclusion formation is enhanced in cells co-transfected with EGFP-huntingtin-(CAG)72 and α-synuclein, a major component of Parkinson's disease aggregates. However, α-synuclein does not form aggregates by itself, nor does it appear in huntingtin inclusions in vitro.
- Published
- 2000
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