SUMO: of branched proteins and nuclear bodies

被引：132

作者：

Seeler, JS ^{[1
]}

Dejean, A ^{[1
]}

机构：

[1] Inst Pasteur, INSERM U 163, Unite Recombust & Express Genet, F-75724 Paris 15, France

来源：

ONCOGENE | 2001年 / 20卷 / 49期

关键词：

SUMO/Sentrin; ubiquitin; PML; SP100; Ubc9;

D O I：

10.1038/sj.onc.1204758

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

SUMO belongs to a growing number of ubiquitin-like proteins that covalently modify their target proteins. Although some evidence supports a role of SUMO modification in regulating protein stability, most studied examples support a model by which SUMO alters the interaction properties of its targets, often affecting their subcellular localization behavior. Examination of the PML nuclear bodies, whose principal components are SUMO-modified, has revealed this modification to be essential for their structural and functional integrity. This and other examples thus support the view that SUMO regulates the stability not of individual proteins, but rather that of entire multiprotein complexes.

引用

页码：7243 / 7249

页数：7

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