Abstract
Protein misfolding and aggregation are common to many disorders, including neurodegenerative diseases referred to as "conformational disorders," suggesting that alterations in the normal protein homeostasis might contribute to pathogenesis. Cells evolved 2 major components of the protein quality control system to deal with misfolded and/or aggregated proteins: molecular chaperones and the ubiquitin proteasome pathway. Recent studies have implicated components of both systems in neurodegenerative diseases such as Alzheimer's, Parkinson's, Huntington's, or the prion diseases. A detailed understanding of how the cellular quality control systems relate to neurodegeneration might lead to the development of novel therapeutic approaches for disorders associated with protein misfolding and aggregation.
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