Ubiquitin-Like Proteins

被引：282

作者：

van der Veen, Annemarthe G. ^{[1
]}

Ploegh, Hidde L. ^{[1
,2
]}

机构：

[1] Whitehead Inst Biomed Res, Cambridge, MA 02142 USA

[2] MIT, Dept Biol, Cambridge, MA 02142 USA

来源：

ANNUAL REVIEW OF BIOCHEMISTRY, VOL 81 | 2012年 / 81卷

关键词：

SUMO; Nedd8; ISG15; autophagy; Urm1; Hub1; INTERFERON-STIMULATED GENE-15; SUMO-BINDING MOTIF; HEPATITIS-C VIRUS; TRANSFER-RNA; IN-VIVO; ISG15; MODIFICATION; STRUCTURAL BASIS; E3; LIGASE; CONJUGATION SYSTEM; MASS-SPECTROMETRY;

D O I：

10.1146/annurev-biochem-093010-153308

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：

The eukaryotic ubiquitin family encompasses nearly 20 proteins that are involved in the posttranslational modification of various macromolecules. The ubiquitin-like proteins (UBLs) that are part of this family adopt the beta-grasp fold that is characteristic of its founding member ubiquitin (Ub). Although structurally related, UBLs regulate a strikingly diverse set of cellular processes, including nuclear transport, proteolysis, translation, autophagy, and antiviral pathways. New UBL substrates continue to be identified and further expand the functional diversity of UBL pathways in cellular homeostasis and physiology. Here, we review recent findings on such novel substrates, mechanisms, and functions of UBLs.

引用

页码：323 / 357

页数：35

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