[HTML][HTML] Aggregated and monomeric α-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function
H Snyder, K Mensah, C Theisler, J Lee… - Journal of Biological …, 2003 - ASBMB
The accumulation of aggregated α-synuclein is thought to contribute to the pathophysiology
of Parkinson's disease, but the mechanism of toxicity is poorly understood. Recent studies
suggest that aggregated proteins cause toxicity by inhibiting the ubiquitin-dependent
proteasomal system. In the present study, we explore how α-synuclein interacts with the
proteasome. The proteasome exists as a 26 S and a 20 S species. The 26 S proteasome is
composed of the 19 S cap and the 20 S core. Aggregated α-synuclein strongly inhibited the …
of Parkinson's disease, but the mechanism of toxicity is poorly understood. Recent studies
suggest that aggregated proteins cause toxicity by inhibiting the ubiquitin-dependent
proteasomal system. In the present study, we explore how α-synuclein interacts with the
proteasome. The proteasome exists as a 26 S and a 20 S species. The 26 S proteasome is
composed of the 19 S cap and the 20 S core. Aggregated α-synuclein strongly inhibited the …