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Plos One : P62, Volume 7

By Yanmin Yang

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Book Id: WPLBN0003957969
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos One : P62, Volume 7  
Author: Yanmin Yang
Volume: Volume 7
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary)
Publication Date:
Publisher: Plos


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Yang, Y. (n.d.). Plos One : P62, Volume 7. Retrieved from

Description : a-Synuclein is the main component of Lewy bodies, the intraneuronal inclusion bodies characteristic of Parkinson’s disease. Although a-synuclein accumulation is caused by inhibition of proteasome and autophagy-lysosome, the degradation of asynuclein inclusions is still unknown. Formation of Lewy body-like inclusions can be replicated in cultured cells by introducing a-synuclein fibrils generated in vitro. We used this cell culture model to investigate the autophagy of asynuclein inclusions and impaired mitochondria. The intracellular a-synuclein inclusions immediately underwent phosphorylation and ubiquitination. Simultaneously they were encircled by an adaptor protein p62/SQSTM1 and directed to the autophagy-lysosome pathway in HEK293 cell line. Most phospho-a-synuclein-positive inclusions were degraded in 24 h, however, lysosomal dysfunction with bafilomycin A1 significantly affected their clearance. Moreover, inhibition of autophagy by Atg-5 siRNA treatment reduced the incorporation of a-synuclein inclusions into LC3-positive autophagosomes. Knockdown experiments demonstrated the requirement of p62 for a-synuclein autophagy. These results demonstrate that a-synuclein inclusions are preferred targets for p62-dependent autophagy. Next, we investigated the autophagic clearance of impaired mitochondria in a-synuclein inclusion-containing cells. Impaired mitochondria were almost completely eliminated after mitochondrial uncoupling even in the presence of a-synuclein inclusions, suggesting that mitochondrial clearance is not prevented by a-synuclein inclusions in HEK293 cells.


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