Molecular chaperone functions in protein folding and proteostasis
- PMID: 23746257
- DOI: 10.1146/annurev-biochem-060208-092442
Molecular chaperone functions in protein folding and proteostasis
Abstract
The biological functions of proteins are governed by their three-dimensional fold. Protein folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically depend on a complex network of molecular chaperones. Disruption of proteostasis is implicated in aging and the pathogenesis of numerous degenerative diseases. In the cytosol, different classes of molecular chaperones cooperate in evolutionarily conserved folding pathways. Nascent polypeptides interact cotranslationally with a first set of chaperones, including trigger factor and the Hsp70 system, which prevent premature (mis)folding. Folding occurs upon controlled release of newly synthesized proteins from these factors or after transfer to downstream chaperones such as the chaperonins. Chaperonins are large, cylindrical complexes that provide a central compartment for a single protein chain to fold unimpaired by aggregation. This review focuses on recent advances in understanding the mechanisms of chaperone action in promoting and regulating protein folding and on the pathological consequences of protein misfolding and aggregation.
Similar articles
-
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.
-
Proteostasis impairment in protein-misfolding and -aggregation diseases.Trends Cell Biol. 2014 Sep;24(9):506-14. doi: 10.1016/j.tcb.2014.05.003. Epub 2014 Jun 16. Trends Cell Biol. 2014. PMID: 24946960 Review.
-
Extracellular chaperones and proteostasis.Annu Rev Biochem. 2013;82:295-322. doi: 10.1146/annurev-biochem-072711-163904. Epub 2013 Jan 23. Annu Rev Biochem. 2013. PMID: 23350744 Review.
-
Molecular chaperones in protein folding and proteostasis.Nature. 2011 Jul 20;475(7356):324-32. doi: 10.1038/nature10317. Nature. 2011. PMID: 21776078 Review.
-
Molecular chaperones in the cytosol: from nascent chain to folded protein.Science. 2002 Mar 8;295(5561):1852-8. doi: 10.1126/science.1068408. Science. 2002. PMID: 11884745 Review.
Cited by
-
Transient heat stress protects from severe endothelial damage and dysfunction during prolonged experimental ex-vivo lung perfusion.Front Immunol. 2024 May 14;15:1390026. doi: 10.3389/fimmu.2024.1390026. eCollection 2024. Front Immunol. 2024. PMID: 38807604 Free PMC article.
-
PRKN-linked familial Parkinson's disease: cellular and molecular mechanisms of disease-linked variants.Cell Mol Life Sci. 2024 May 20;81(1):223. doi: 10.1007/s00018-024-05262-8. Cell Mol Life Sci. 2024. PMID: 38767677 Free PMC article. Review.
-
STORM Super-Resolution Visualization of Self-Assembled γPFD Chaperone Ultrastructures in Methanocaldococcus jannaschii.Nano Lett. 2024 May 22;24(20):6078-6083. doi: 10.1021/acs.nanolett.4c01043. Epub 2024 May 9. Nano Lett. 2024. PMID: 38723608 Free PMC article.
-
Intranasal Administration of GRP78 Protein (HSPA5) Confers Neuroprotection in a Lactacystin-Induced Rat Model of Parkinson's Disease.Int J Mol Sci. 2024 Apr 2;25(7):3951. doi: 10.3390/ijms25073951. Int J Mol Sci. 2024. PMID: 38612761 Free PMC article.
-
Mitigation Potential of Herbal Extracts and Constituent Bioactive Compounds on Salmonella in Meat-Type Poultry.Animals (Basel). 2024 Apr 3;14(7):1087. doi: 10.3390/ani14071087. Animals (Basel). 2024. PMID: 38612326 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
