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小泛素样修饰蛋白(SUMO):修饰历程

SUMO: a history of modification.

作者信息

Hay Ronald T

机构信息

Centre for Biomolecular Sciences, School of Biology, University of St Andrews, North Haugh, St. Andrews KY16 9ST, Scotland.

出版信息

Mol Cell. 2005 Apr 1;18(1):1-12. doi: 10.1016/j.molcel.2005.03.012.

Abstract

The small ubiquitin-like modifier (SUMO) is covalently linked to a variety of proteins and is deconjugated by SUMO-specific proteases. A characteristic of SUMO modification is that the biological consequences of conjugation do not appear proportionate to the small fraction of substrate that is modified. SUMO conjugation appears to alter the long-term fate of the modified protein even though the SUMO may be rapidly deconjugated. Thus an unmodified protein with a history of SUMO modification may have different properties from a protein that never has been modified. Here, the diverse effects of SUMO modification are discussed and models proposed to explain SUMO actions.

摘要

小泛素样修饰物(SUMO)与多种蛋白质共价连接,并由SUMO特异性蛋白酶去共轭。SUMO修饰的一个特点是,共轭的生物学后果似乎与被修饰底物的一小部分不成比例。尽管SUMO可能会迅速去共轭,但SUMO共轭似乎会改变被修饰蛋白质的长期命运。因此,具有SUMO修饰历史的未修饰蛋白质可能具有与从未被修饰过的蛋白质不同的特性。在此,讨论了SUMO修饰的多种效应,并提出了解释SUMO作用的模型。

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