
Polyglutamine domain proteins with expanded repeats bind neurofilament, altering the neurofilament network.
Proteins with expanded polyglutamine (polyQ) repeats cause eight inherited neurodegenerative diseases. Nuclear and cytoplasmic polyQ protein is a common feature of these diseases, but its role in cell death remains debatable. Since the neuronal intermediate filament network is composed of neurofilament (NF) and NF abnormalities occur in neurodegenerative diseases, we examined whether pathologic-length polyQ domain proteins interact with NF. We expressed polyQ-green fluorescent fusion proteins (GFP) in a neuroblast cell line, TR1. Pathologic-length polyQ-GFP fusion proteins form large cytoplasmic aggregates surrounded by neurofilament. Immunoisolation of pathologic-length polyQ proteins co-isolated 68 kD NF protein demonstrating molecular interaction. These observations suggest that polyQ interaction with NF is important in the pathogenesis of the polyglutamine repeat diseases.
Duke Scholars
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Related Subject Headings
- Transfection
- Repetitive Sequences, Amino Acid
- Recombinant Fusion Proteins
- Peptides
- Neurons
- Neurofilament Proteins
- Neurofibrils
- Molecular Sequence Data
- Luminescent Proteins
- Green Fluorescent Proteins
Citation

Published In
DOI
ISSN
Publication Date
Volume
Start / End Page
Location
Related Subject Headings
- Transfection
- Repetitive Sequences, Amino Acid
- Recombinant Fusion Proteins
- Peptides
- Neurons
- Neurofilament Proteins
- Neurofibrils
- Molecular Sequence Data
- Luminescent Proteins
- Green Fluorescent Proteins