Abstract
In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborate quality-control strategies have evolved to counter these inevitable mishaps. Recent reports describe the removal of aggregates from the cytosol; reveal mechanisms for protein quality control in the endoplasmic reticulum; and provide new insight into two classes of molecular chaperones, the Hsp70 system and the AAA+ (Hsp100) unfoldases.
MeSH terms
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Adenosine Triphosphate / metabolism
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Allosteric Regulation / physiology
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Animals
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Cytosol / metabolism
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Endopeptidase Clp
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Endoplasmic Reticulum / metabolism
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HSP70 Heat-Shock Proteins / metabolism
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Heat-Shock Proteins / metabolism
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Humans
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Molecular Chaperones / metabolism*
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Protein Biosynthesis / physiology*
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Protein Folding*
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Proteins / chemistry
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Proteins / metabolism*
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Protozoan Proteins / metabolism
Substances
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HSP70 Heat-Shock Proteins
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Heat-Shock Proteins
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Molecular Chaperones
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Proteins
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Protozoan Proteins
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Adenosine Triphosphate
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Endopeptidase Clp
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ClpB protein, Leishmania