Journal
TRENDS IN NEUROSCIENCES
Volume 31, Issue 10, Pages 521-528Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tins.2008.07.004
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Funding
- National Institutes of Neurological Disorders and Stroke [NS056609, NS38712]
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [F31NS056609, R01NS038712] Funding Source: NIH RePORTER
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Polyglutamine diseases are a major cause of neurodegeneration worldwide. Recent studies highlight the importance of protein quality control mechanisms in regulating polyglutamine-induced toxicity. Here we discuss a model of disease pathogenesis that integrates current understanding of the role of protein folding in polyglutamine disease with emerging evidence that alterations in native protein interactions contribute to toxicity. We also incorporate new findings on other age-related neurodegenerative diseases in an effort to explain how protein aggregation and normal aging processes might be involved in polyglutamine disease pathogenesis.
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