Cells have to cope with stressful conditions and adapt to changing environments. Heat stress, heavy metal ions or UV stress induce damage to cellular proteins and disturb the balanced status of the proteome. The adjusted balance between folded and folding proteins, called protein homoeostasis, is required for every aspect of cellular functionality. Protective proteins called chaperones are expressed under extreme conditions in order to prevent aggregation of cellular proteins and safeguard protein quality. These chaperones co-operate during de novo folding, refolding and disaggregation of damaged proteins and in many cases refold them to their functional state. Even under physiological conditions these machines support protein homoeostasis and maintain the balance between de novo folding and degradation. Mutations generating unstable proteins, which are observed in numerous human diseases such as Alzheimer's disease, Huntington's disease, amyotrophic lateral sclerosis and cystic fibrosis, also challenge the protein quality control system. A better knowledge of how the protein homoeostasis system is regulated will lead to an improved understanding of these diseases and provide potential targets for therapy.
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August 2014
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Review Article|
August 18 2014
Protein folding, misfolding and quality control: the role of molecular chaperones
Katharina Papsdorf;
Katharina Papsdorf
Department Chemie, Lehrstuhl für Biotechnologie, Lichtenbergstrasse 4, 85748 Garching, Germany
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Klaus Richter
Klaus Richter
1
Department Chemie, Lehrstuhl für Biotechnologie, Lichtenbergstrasse 4, 85748 Garching, Germany
1To whom correspondence should be addressed (email klaus.richter@tum.de).
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Publisher: Portland Press Ltd
Online ISSN: 1744-1358
Print ISSN: 0071-1365
© The Authors Journal compilation © 2014 Biochemical Society
2014
Essays Biochem (2014) 56: 53–68.
Citation
Sarah Perrett, Katharina Papsdorf, Klaus Richter; Protein folding, misfolding and quality control: the role of molecular chaperones. Essays Biochem 18 August 2014; 56 53–68. doi: https://doi.org/10.1042/bse0560053
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