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Molecular chaperones in protein folding and proteostasis

Hartl, F. Ulrich, Bracher, Andreas, Hayer-Hartl, Manajit·2011·Nature
DOI 10.1038/nature10317
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Abstract

Most proteins must fold into defined three-dimensional structures to gain functional activity. But in the cellular environment, newly synthesized proteins are at great risk of aberrant folding and aggregation, potentially forming toxic species. To avoid these dangers, cells invest in a complex network of molecular chaperones, which use ingenious mechanisms to prevent aggregation and promote efficient folding. Because protein molecules are highly dynamic, constant chaperone surveillance is required to ensure protein homeostasis (proteostasis). Recent advances suggest that an age-related decline in proteostasis capacity allows the manifestation of various protein-aggregation diseases, including Alzheimer's disease and Parkinson's disease. Interventions in these and numerous other pathological states may spring from a detailed understanding of the pathways underlying proteome maintenance.

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  • Proteostasis involves mechanisms for the stabilization of correctly folded proteins, most prominently the heat-shock family of proteins, and mechanisms for the degradation of proteins by the proteasome or the lysosome.

    “Proteostasis involves mechanisms for the stabilization of correctly folded proteins, most prominently the heat-shock family of proteins, and mechanisms for the degradation of proteins by the proteasome or the lysosome (Hartl et al., 2011; Koga et al., 2011; Mizushima et al., 2008).”

    From The Hallmarks of Aging (2013) · cites this paper as Hartl et al., 2011

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Authors
Hartl, F. U., Bracher, A., & Hayer-Hartl, M.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2011-07
Volume
475
Issue
7356
Pages
324-332
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature10317
Cited by
3,381
References
14
Language
en
Licence
www.springer.com/tdm (tdm)

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