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Molecular Chaperone Functions in Protein Folding and Quality Control

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The past two decades have witnessed a paradigm shift in our understanding of cellular protein folding. While the three-dimensional structures of functional proteins are determined by their amino acid sequences, it is now firmly established that in the cell many proteins depend on molecular chaperones to reach their folded states efficiently and on a biologically relevant time scale. Assistance of protein folding is provided by different types of chaperone which act to prevent misfolding and aggregation, often in an ATP -dependent mechanism. Molecular chaperones also cooperate with the degradation machinery (ubiquitin-proteasome system and autophagy) in the removal of terminally misfolded proteins.

Once folded, many proteins continue to require chaperones to retain their functional states, especially under conditions of cell stress. Failure of the chaperone network to maintain proteostasis, i.e. the conformational integrity of the cellular proteome, facilitates the manifestation of diseases in which proteins misfold and are deposited as aggregates, such as Parkinsons and Huntingtons disease. Proteostasis undergoes a decline during aging, presumably explaining why age is a major risk factor of neurodegenerative pathologies.

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