Cellular strategies for controlling protein aggregation

被引:678
作者
Tyedmers, Jens [1 ]
Mogk, Axel [1 ]
Bukau, Bernd [1 ]
机构
[1] Univ Heidelberg ZMBH, Zentrum Mol Biol, DKFZ ZMBH Alliance, D-69120 Heidelberg, Germany
关键词
INCLUSION-BODY FORMATION; VALOSIN-CONTAINING PROTEIN; HEAT-SHOCK PROTEINS; MEDIATED K63-LINKED POLYUBIQUITINATION; SACCHAROMYCES-CEREVISIAE HSP104; UBIQUITIN-PROTEASOME SYSTEM; PLUS CHAPERONE CLPB; QUALITY-CONTROL; ESCHERICHIA-COLI; DAMAGED PROTEINS;
D O I
10.1038/nrm2993
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The aggregation of misfolded proteins is associated with the perturbation of cellular function, ageing and various human disorders. Mounting evidence suggests that protein aggregation is often part of the cellular response to an imbalanced protein homeostasis rather than an unspecific and uncontrolled dead-end pathway. It is a regulated process in cells from bacteria to humans, leading to the deposition of aggregates at specific sites. The sequestration of misfolded proteins in such a way is protective for cell function as it allows for their efficient solubilization and refolding or degradation by components of the protein quality-control network. The organized aggregation of misfolded proteins might also allow their asymmetric distribution to daughter cells during cell division.
引用
收藏
页码:777 / 788
页数:12
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