Abstract
Cells require a protein quality control (PQC) system to obtain a correct balance between folding and the degradation of incorrectly folded or misfolded proteins. This system maintains protein homeostasis and is essential for life. Key components of the PQC are molecular chaperones, which compose a ubiquitous class of proteins that mediate protein quality control by aiding in both the correct folding of proteins and the elimination of proteins that are misfolded due to cellular stress or mutation. Recent studies showed that protein homeostasis has an important role in nutrition and aging, increasing the relevance of the heat shock response to human health. This review summarizes our current knowledge of the molecular chaperone system and its role in protein homeostasis.
Keywords: Heat shock protein, molecular chaperones, protein homeostasis, protein quality control, protein folding, homeostasis, nutrition, aging, enzymes, IUPs, cellular stress, mutations, solvent, type II diabetes, Parkinson's disease, amyloid fibrils, folded globular proteins, Chaperones, heat-shock proteins, degradation, phenotypes, Holdases, ATP hydrolysis, Hsp90, sHsp, cellular localization, NBD, SBD, E. coli, C-terminal domains, TPR, MEEVD domain, Hsc70, Hsp100, SmHsps, GroEL, TriC, TCP, RNA, Arabidopsis thaliana, HSR, Sir, lysozyme, MAPK, UPR, ER, BiP, ERAD, PQCHeat shock protein, molecular chaperones, protein homeostasis, protein quality control, protein folding, homeostasis, nutrition, aging, enzymes, IUPs, cellular stress, mutations, solvent, type II diabetes, Parkinson's disease, amyloid fibrils, folded globular proteins, Chaperones, heat-shock proteins, degradation, phenotypes, Holdases, ATP hydrolysis, Hsp90, sHsp, cellular localization, NBD, SBD, E. coli, C-terminal domains, TPR, MEEVD domain, Hsc70, Hsp100, SmHsps, GroEL, TriC, TCP, RNA, Arabidopsis thaliana, HSR, Sir, lysozyme, MAPK, UPR, ER, BiP, ERAD, PQC
Protein & Peptide Letters
Title: An Overview of the Role of Molecular Chaperones in Protein Homeostasis
Volume: 18 Issue: 2
Author(s): Ana O. Tiroli-Cepeda and Carlos H.I. Ramos
Affiliation:
Keywords: Heat shock protein, molecular chaperones, protein homeostasis, protein quality control, protein folding, homeostasis, nutrition, aging, enzymes, IUPs, cellular stress, mutations, solvent, type II diabetes, Parkinson's disease, amyloid fibrils, folded globular proteins, Chaperones, heat-shock proteins, degradation, phenotypes, Holdases, ATP hydrolysis, Hsp90, sHsp, cellular localization, NBD, SBD, E. coli, C-terminal domains, TPR, MEEVD domain, Hsc70, Hsp100, SmHsps, GroEL, TriC, TCP, RNA, Arabidopsis thaliana, HSR, Sir, lysozyme, MAPK, UPR, ER, BiP, ERAD, PQCHeat shock protein, molecular chaperones, protein homeostasis, protein quality control, protein folding, homeostasis, nutrition, aging, enzymes, IUPs, cellular stress, mutations, solvent, type II diabetes, Parkinson's disease, amyloid fibrils, folded globular proteins, Chaperones, heat-shock proteins, degradation, phenotypes, Holdases, ATP hydrolysis, Hsp90, sHsp, cellular localization, NBD, SBD, E. coli, C-terminal domains, TPR, MEEVD domain, Hsc70, Hsp100, SmHsps, GroEL, TriC, TCP, RNA, Arabidopsis thaliana, HSR, Sir, lysozyme, MAPK, UPR, ER, BiP, ERAD, PQC
Abstract: Cells require a protein quality control (PQC) system to obtain a correct balance between folding and the degradation of incorrectly folded or misfolded proteins. This system maintains protein homeostasis and is essential for life. Key components of the PQC are molecular chaperones, which compose a ubiquitous class of proteins that mediate protein quality control by aiding in both the correct folding of proteins and the elimination of proteins that are misfolded due to cellular stress or mutation. Recent studies showed that protein homeostasis has an important role in nutrition and aging, increasing the relevance of the heat shock response to human health. This review summarizes our current knowledge of the molecular chaperone system and its role in protein homeostasis.
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Cite this article as:
O. Tiroli-Cepeda Ana and H.I. Ramos Carlos, An Overview of the Role of Molecular Chaperones in Protein Homeostasis, Protein & Peptide Letters 2011; 18 (2) . https://dx.doi.org/10.2174/092986611794475093
DOI https://dx.doi.org/10.2174/092986611794475093 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |

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