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α-synuclein interacts with SOD1 and promotes its oligomerization.
- Source :
-
Molecular Neurodegeneration . 12/8/2015, Vol. 10, p1-16. 16p. 1 Color Photograph, 1 Black and White Photograph, 6 Graphs. - Publication Year :
- 2015
-
Abstract
- Background: Parkinson's disease (PD) and amyotrophic lateral sclerosis (ALS) are both neurodegenerative diseases leading to impaired execution of movement. α-Synuclein plays a central role in the pathogenesis of PD whereas Cu, Zn superoxide dismutase (SOD1) is a key player in a subset of familial ALS cases. Under pathological conditions both α-synuclein and SOD1 form oligomers and fibrils. In this study we investigated the possible molecular interaction of α-synuclein and SOD1 and its functional and pathological relevance. Results: Using a protein-fragment complementation approach and co-IP, we found that α-synuclein and SOD1 physically interact in living cells, human erythrocytes and mouse brain tissue. Additionally, our data show that disease related mutations in α-synuclein (A30P, A53T) and SOD1 (G85R, G93A) modify the binding of α-synuclein to SOD1. Notably, α-synuclein accelerates SOD1 oligomerization independent of SOD1 activity. Conclusion: This study provides evidence for a novel interaction of α-synuclein and SOD1 that might be relevant for neurodegenerative diseases. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 17501326
- Volume :
- 10
- Database :
- Academic Search Index
- Journal :
- Molecular Neurodegeneration
- Publication Type :
- Academic Journal
- Accession number :
- 111521107
- Full Text :
- https://doi.org/10.1186/s13024-015-0062-3