Department of Biology and BioX Program, Stanford University, Stanford, California 94305, USA.
Cold Spring Harb Perspect Biol. 2011 Aug 1;3(8):a004374. doi: 10.1101/cshperspect.a004374.
Eukaryotic cells must contend with a continuous stream of misfolded proteins that compromise the cellular protein homeostasis balance and jeopardize cell viability. An elaborate network of molecular chaperones and protein degradation factors continually monitor and maintain the integrity of the proteome. Cellular protein quality control relies on three distinct yet interconnected strategies whereby misfolded proteins can either be refolded, degraded, or delivered to distinct quality control compartments that sequester potentially harmful misfolded species. Molecular chaperones play a critical role in determining the fate of misfolded proteins in the cell. Here, we discuss the spatial and temporal organization of cellular quality control strategies and their implications for human diseases linked to protein misfolding and aggregation.
真核细胞必须应对不断出现的错误折叠蛋白质，这些蛋白质破坏了细胞的蛋白质平衡并危及细胞活力。一个精心构建的分子伴侣和蛋白降解因子网络不断监测和维持蛋白质组的完整性。细胞的蛋白质质量控制依赖于三种不同但相互关联的策略，其中错误折叠的蛋白质可以被重折叠、降解，或者被递送到不同的质量控制隔室，从而隔离潜在有害的错误折叠物质。分子伴侣在决定细胞中错误折叠蛋白质的命运方面发挥着关键作用。在这里，我们讨论了细胞质量控制策略的空间和时间组织及其对与蛋白质错误折叠和聚集相关的人类疾病的影响。
