The predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradation

被引:250
作者
Weissman, Allan M. [1 ]
Shabek, Nitzan [2 ,3 ]
Ciechanover, Aaron [2 ,3 ]
机构
[1] NCI, Lab Prot Dynam & Signalling, Frederick, MD 21702 USA
[2] Technion Israel Inst Technol, Canc & Vasc Biol Res Ctr, Rappaport Fac Med, IL-31096 Haifa, Israel
[3] Technion Israel Inst Technol, Res Inst, IL-31096 Haifa, Israel
基金
以色列科学基金会; 美国国家卫生研究院;
关键词
ANAPHASE-PROMOTING COMPLEX; RETICULUM-ASSOCIATED DEGRADATION; PEROXISOMAL IMPORT RECEPTOR; POLYCOMB PROTEIN RING1B; ENDOPLASMIC-RETICULUM; DEUBIQUITINATING ENZYME; 26S PROTEASOME; E3; LIGASE; IN-VITRO; S-PHASE;
D O I
10.1038/nrm3173
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Ubiquitylation (also known as ubiquitination) regulates essentially all of the intracellular processes in eukaryotes through highly specific modification of numerous cellular proteins, which is often tightly regulated in a spatial and temporal manner. Although most often associated with proteasomal degradation, ubiquitylation frequently serves non-proteolytic functions. In light of its central roles in cellular regulation, it has not been surprising to find that many of the components of the ubiquitin system itself are regulated by ubiquitylation. This observation has broad implications for pathophysiology.
引用
收藏
页码:605 / 620
页数:16
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