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Preventing ?-synuclein aggregation: The role of the small heat-shock molecular chaperone proteins.

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Biochim Biophys Acta 2014 Jun; 1842(9):1830-1843

Authors: Dezerae Cox, John A Carver, Heath Ecroyd

Protein homeostasis, or proteostasis, is the process of maintaining the conformational and functional integrity of the proteome. The failure of proteostasis can result in the accumulation of non-native proteins leading to their aggregation and deposition in cells and in tissues. The amyloid fibrillar aggregation of the protein ?-synuclein into Lewy bodies and Lewy neuritis is associated with neurodegenerative diseases classified as ?-synucleinopathies, which include Parkinson's disease and dementia with Lewy bodies. The small heat-shock proteins (sHsps) are molecular chaperones that are one of the cell's first lines of defence against protein aggregation. They act to stabilise partially folded protein intermediates, in an ATP-independent manner, to maintain cellular proteostasis under stress conditions. Thus, the sHsps appear ideally suited to protect against ?-synuclein aggregation, yet these fail to do so in the context of the ?-synucleinopathies. This review discusses how sHsps interact with ?-synuclein to prevent its aggregation and, in doing so, highlights the multi-faceted nature of the mechanisms used by sHsps to prevent the fibrillar aggregation of proteins. It also examines what factors may contribute to ?-synuclein escaping the sHsp chaperones in the context of the ?-synucleinopathies.

PMID: 24973551 [PubMed - as supplied by publisher]

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