Journal
JOURNAL OF NEUROSCIENCE
Volume 35, Issue 41, Pages 13853-13859Publisher
SOC NEUROSCIENCE
DOI: 10.1523/JNEUROSCI.2600-15.2015
Keywords
chaperone; heat shock proteins; protein misfolding; proteostasis; neurodegeneration; Parkinson's disease
Categories
Funding
- National Institutes of Health [AG045741, DA05084, GM099836, DP2OD002177, NS067354, NS092829, DK102635, MH103848, NS073899, NS073740]
- Muscular Dystrophy Association [MDA277268]
- Target ALS
- Amyloidosis Foundation
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Cellular protein homeostasis (proteostasis) maintains the integrity of the proteome and includes protein synthesis, folding, oligomerization, and turnover; chaperone proteins assist with all of these processes. Neurons appear to be especially susceptible to failures in proteostasis, and this is now increasingly recognized as a major origin of neurodegenerative disease. This review, based on a mini-symposium presented at the 2015 Society for Neuroscience meeting, describes new work in the area of neuronal proteostasis, with a specific focus on the roles and therapeutic uses of protein chaperones. We first present a brief review of protein misfolding and aggregation in neurodegenerative disease. We then discuss different aspects of chaperone control of neuronal proteostasis on topics ranging from chaperone engineering, to chaperone-mediated blockade of protein oligomerization and cytotoxicity, to the potential rescue of neurodegenerative processes using modified chaperone proteins.
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