Molecular chaperones in protein folding and proteostasis
- PMID: 21776078
- DOI: 10.1038/nature10317
Molecular chaperones in protein folding and proteostasis
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.
Similar articles
-
Molecular chaperone functions in protein folding and proteostasis.Annu Rev Biochem. 2013;82:323-55. doi: 10.1146/annurev-biochem-060208-092442. Annu Rev Biochem. 2013. PMID: 23746257 Review.
-
In vivo aspects of protein folding and quality control.Science. 2016 Jul 1;353(6294):aac4354. doi: 10.1126/science.aac4354. Science. 2016. PMID: 27365453 Review.
-
Biological and chemical approaches to diseases of proteostasis deficiency.Annu Rev Biochem. 2009;78:959-91. doi: 10.1146/annurev.biochem.052308.114844. Annu Rev Biochem. 2009. PMID: 19298183 Review.
-
Carrying Excess Baggage Can Slowdown Life: Protein Clearance Machineries That Go Awry During Aging and the Relevance of Maintaining Them.Mol Neurobiol. 2022 Feb;59(2):821-840. doi: 10.1007/s12035-021-02640-2. Epub 2021 Nov 18. Mol Neurobiol. 2022. PMID: 34792731 Review.
-
Proteostasis and the aging proteome in health and disease.J Gerontol A Biol Sci Med Sci. 2014 Jun;69 Suppl 1(Suppl 1):S33-8. doi: 10.1093/gerona/glu049. J Gerontol A Biol Sci Med Sci. 2014. PMID: 24833584 Free PMC article. Review.
Cited by
-
O-GlcNAc modification of HSP27 alters its protein interactions and promotes refolding of proteins through the BAG3/HSP70 co-chaperone.Protein Sci. 2024 Oct;33(10):e5173. doi: 10.1002/pro.5173. Protein Sci. 2024. PMID: 39291732 Free PMC article.
-
Rationally modified SNX-class Hsp90 inhibitors disrupt extracellular fibronectin assembly without intracellular Hsp90 activity.RSC Med Chem. 2024 Sep 2. doi: 10.1039/d4md00501e. Online ahead of print. RSC Med Chem. 2024. PMID: 39290382 Free PMC article.
-
Reversible cold-induced lens opacity in a hibernator reveals a molecular target for treating cataracts.J Clin Invest. 2024 Sep 17;134(18):e169666. doi: 10.1172/JCI169666. J Clin Invest. 2024. PMID: 39286982 Free PMC article.
-
HSF1 is required for cellular adaptation to daily temperature fluctuations.Sci Rep. 2024 Sep 12;14(1):21361. doi: 10.1038/s41598-024-72415-x. Sci Rep. 2024. PMID: 39266731 Free PMC article.
-
Heat shock proteins as hallmarks of cancer: insights from molecular mechanisms to therapeutic strategies.J Hematol Oncol. 2024 Sep 4;17(1):81. doi: 10.1186/s13045-024-01601-1. J Hematol Oncol. 2024. PMID: 39232809 Free PMC article. Review.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources