Journal
JOURNAL OF NEUROCHEMISTRY
Volume 137, Issue 4, Pages 489-505Publisher
WILEY
DOI: 10.1111/jnc.13575
Keywords
aging; aggregation; autophagy; chaperones; heat-shock proteins; ubiquitin-proteasome system
Categories
Funding
- ARC DECRA
- ARC Future Fellowship [FT110100586]
- NHMRC Research Fellowship [APP1019833]
- NHMRC
- Garvan Research Foundation
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A characteristic of many neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD), and amyotrophic lateral sclerosis (ALS), is the aggregation of specific proteins into protein inclusions and/or plaques in degenerating brains. While much of the aggregated protein consists of disease specific proteins, such as amyloid-beta, alpha-synuclein, or superoxide dismutase1 (SOD1), many other proteins are known to aggregate in these disorders. Although the role of protein aggregates in the pathogenesis of neurodegenerative diseases remains unknown, the ubiquitous association of misfolded and aggregated proteins indicates that significant dysfunction in protein homeostasis (proteostasis) occurs in these diseases. Proteostasis is the concept that the integrity of the proteome is in fine balance and requires proteins in a specific conformation, concentration, and location to be functional. In this review, we discuss the role of specific mechanisms, both inside and outside cells, which maintain proteostasis, including molecular chaperones, protein degradation pathways, and the active formation of inclusions, in neurodegenerative diseases associated with protein aggregation.
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