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?-synuclein interacts with SOD1 and promotes its oligomerization.

ABSTRACT: Parkinson's disease (PD) and amyotrophic lateral sclerosis (ALS) are both neurodegenerative diseases leading to impaired execution of movement. ?-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 ?-synuclein and SOD1 form oligomers and fibrils. In this study we investigated the possible molecular interaction of ?-synuclein and SOD1 and its functional and pathological relevance.Using a protein-fragment complementation approach and co-IP, we found that ?-synuclein and SOD1 physically interact in living cells, human erythrocytes and mouse brain tissue. Additionally, our data show that disease related mutations in ?-synuclein (A30P, A53T) and SOD1 (G85R, G93A) modify the binding of ?-synuclein to SOD1. Notably, ?-synuclein accelerates SOD1 oligomerization independent of SOD1 activity.This study provides evidence for a novel interaction of ?-synuclein and SOD1 that might be relevant for neurodegenerative diseases.

SUBMITTER: Helferich AM 

PROVIDER: S-EPMC4672499 | biostudies-other | 2015 Dec

REPOSITORIES: biostudies-other

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<h4>Background</h4>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 fun  ...[more]

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