Function and regulation of SUMO proteases

被引：584

作者：

Hickey, Christopher M. ^{[1
]}

Wilson, Nicole R. ^{[1
]}

Hochstrasser, Mark ^{[1
]}

机构：

[1] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA

来源：

NATURE REVIEWS MOLECULAR CELL BIOLOGY | 2012年 / 13卷 / 12期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

AXIN-BINDING PROTEIN; UBIQUITIN E3 LIGASE; TRANSCRIPTIONAL REPRESSION; SACCHAROMYCES-CEREVISIAE; SUMOYLATED PROTEINS; CRYSTAL-STRUCTURE; REDOX REGULATION; STRUCTURAL BASIS; RIBOSOMAL-RNA; ISOPEPTIDASE;

D O I：

10.1038/nrm3478

中图分类号：

Q2 [细胞生物学];

学科分类号：

071013 [干细胞生物学];

摘要：

Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins is highly dynamic, and both SUMO-protein conjugation and cleavage can be regulated. Protein desumoylation is carried out by SUMO proteases, which control cellular mechanisms ranging from transcription and cell division to ribosome biogenesis. Recent advances include the discovery of two novel classes of SUMO proteases, insights regarding SUMO protease specificity, and revelations of previously unappreciated SUMO protease functions in several key cellular pathways. These developments, together with new connections between SUMO proteases and the recently discovered SUMO-targeted ubiquitin ligases (STUbLs), make this an exciting period to study these enzymes.

引用

页码：755 / 766

页数：12

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