SUMO/sentrin: protein modifiers regulating important cellular functions
SUMO/sentrin: protein modifiers regulating important cellular functions
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DOI：
10.1139/bcb-77-4-299
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发表时间：
1999-01-01
影响因子：
2.9
通讯作者：
Tanguay, RM
中科院分区：
文献类型：
--
作者：
Kretz-Remy, C;Tanguay, RM
蛋白质功能的调节可以通过翻译后的蛋白质修饰来实现。研究最多的修饰之一是与泛素的偶联，泛素主要针对底物蛋白，由26s蛋白酶体降解。最近，SUMO/sentrin，一种泛素样蛋白被表征。这种进化保守的蛋白质以一种与泛素相似但不完全相同的方式与特定蛋白质结合，似乎也参与蛋白质定位或功能的调节。越来越多的SUMO/sentrin底物目前被描述。我们在这里重点讨论了SUMO修饰的三个主要底物：RanGAP1、PML和I κ B α蛋白。这些不同的例子说明了SUMO偶联如何参与控制细胞内关键蛋白的水平或调节亚细胞定位和核细胞质运输。
Regulation of protein functions can be achieved by posttranslational protein modifications. One of the most studied modifications has been conjugation to ubiquitin, which mainly targets substrate proteins for degradation by the 26 S proteasome. Recently, SUMO/sentrin, a ubiquitin-like protein has been characterized. This evolutionary conserved protein is conjugated to specific proteins in a way similar, but not identical, to ubiquitin and seems also to be involved in the regulation of protein localization or function. An increasing number of SUMO/sentrin substrates are currently described. We focus here on three major substrates of modification by SUMO: RanGAP1, PML, and I kappa B alpha proteins. These different examples illustrate how SUMO conjugation may be involved in the control of the level of critical proteins within the cell or in the modulation of subcellular localization and nucleocytoplasmic trafficking.