Role of the ubiquitin––proteasome system and autophagy in polyglutamine neurodegenerative diseases. (January 2010)

• Record Type: Journal Article
• Authors: Jana, Nihar Ranjan
• Is Part Of: Future neurology. Volume 5:Number 1(2010)
• Page Start: 105
• Page End: 112
• Publication Date: 2010-01
• Subjects: autophagy -- neurodegeneration -- polyglutamine -- proteasome -- ubiquitin; Neurology -- Research -- Periodicals; 611.8005
• DOI: 10.2217/fnl.09.69
• Languages: English
• ISSNs: 1479-6708

Abstract

The accumulation of intracellular protein aggregates is a prominent feature of many late-onset neurodegenerative disorders, including polyglutamine neurodegenerative diseases. Appearance of aggregates of the misfolded mutant disease proteins indicate that the degradative pathways of the cell are failing to efficiently clear them and are being progressively overwhelmed, which could eventually lead to neuronal dysfunction and neurodegeneration. Cellular pathways for degrading misfolded and aggregated-prone proteins include the ubiquitin––proteasome system and autophagy. This article reviews recent studies that have shown a critical role of the ubiquitin––proteasome system and autophagy in the pathogenesis of polyglutamine diseases. Understanding the role of these two pathways in disease pathogenesis could open up a new attractive therapeutic avenue for polyglutamine and other related neurodegenerative disorders.