Molecular chaperones and protein quality control
Bernd Bukau1, Jonathan Weissman, Arthur Horwich
1Zentrum fur Molekulare Biologie, Universität Heidelberg, 69120 Heidelberg, Germany.
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.
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