Bukau Bernd, Weissman Jonathan, Horwich Arthur
Zentrum fur Molekulare Biologie, Universität Heidelberg, 69120 Heidelberg, Germany.
Cell. 2006 May 5;125(3):443-51. doi: 10.1016/j.cell.2006.04.014.
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.
在活细胞中，新合成的和预先存在的多肽链都始终面临错误折叠和聚集的风险。鉴于错误折叠形式的多样性，已经进化出了精细的质量控制策略来应对这些不可避免的意外情况。最近的报告描述了从细胞质中清除聚集体的过程；揭示了内质网中蛋白质质量控制的机制；并为两类分子伴侣，即Hsp70系统和AAA +（Hsp100）解折叠酶提供了新的见解。
