The Ubiquitin-Proteasome System of Saccharomyces cerevisiae

被引：309
|
作者：
Finley, Daniel [2 ]
Ulrich, Helle D. [1 ]
Sommer, Thomas [3 ]
Kaiser, Peter [4 ]
机构：
[1] Imperial Canc Res Fund, Clare Hall Labs, Canc Res UK London Res Inst, S Mimms EN6 3LD, Herts, England
[2] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA
[3] Max Delbruck Ctr Mol Med, D-13125 Berlin, Germany
[4] Univ Calif Irvine, Dept Biol Chem, Irvine, CA 92697 USA
来源：
GENETICS | 2012年 / 192卷 / 02期
基金：
美国国家卫生研究院;
关键词：
N-END RULE; RNA-POLYMERASE-II; PROTEIN-QUALITY CONTROL; DOA4 DEUBIQUITINATING ENZYME; MULTIVESICULAR BODY PATHWAY; SISTER-CHROMATID SEPARATION; NUCLEOTIDE EXCISION-REPAIR; HISTONE H2B UBIQUITYLATION; 19S REGULATORY PARTICLE; DNA-DAMAGE BYPASS;
D O I：
10.1534/genetics.112.140467
中图分类号：
Q3 [遗传学];
学科分类号：
071007 ; 090102 ;
摘要：
Protein modifications provide cells with exquisite temporal and spatial control of protein function. Ubiquitin is among the most important modifiers, serving both to target hundreds of proteins for rapid degradation by the proteasome, and as a dynamic signaling agent that regulates the function of covalently bound proteins. The diverse effects of ubiquitylation reflect the assembly of structurally distinct ubiquitin chains on target proteins. The resulting ubiquitin code is interpreted by an extensive family of ubiquitin receptors. Here we review the components of this regulatory network and its effects throughout the cell.
引用
收藏
页码：319 / 360
页数：42
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