Cellular strategies for making monoubiquitin signals.
Cellular strategies for making monoubiquitin signals.
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DOI：
10.3109/10409238.2011.620943
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发表时间：
2012-01
影响因子：
6.5
通讯作者：
Ye Y
中科院分区：
文献类型：
--
作者：
Ramanathan HN;Ye Y
泛素对蛋白质的翻译后修饰调节了多种真核细胞过程。泛素可以作为单一部分（单泛素化）或作为异肽键连接的链（多泛素化）与底物缀合，产生一系列泛素信号。已经确定，单泛素化可以在许多生物过程中发挥重要作用，如基因转录的调节，蛋白质运输和DNA修复。令人惊讶的是，关于monoubiquitin信号在细胞中产生的机制知之甚少。在这里，我们讨论了潜在的细胞策略产生monoubiquitinated蛋白质使用几个，相对较好的特点monoubiquitinated蛋白质的例子。这些策略包括将泛素化与低亲和力泛素结合偶联，使用单泛素化专用的E2缀合酶，以及限制泛素链延伸。这些原则中的一些可能适用于涉及泛素样蛋白（UBL）的蛋白质修饰，其通常以单体形式出现。
Post-translational modification of proteins with ubiquitin regulates a variety of eukaryotic cellular processes. Ubiquitin can be conjugated to substrates either as a single moiety (monoubiquitination) or as isopeptide bond-linked chains (polyubiquitination), creating an array of ubiquitin signals. It has been established that monoubiquitination can serve important functions in many biological processes such as the regulation of gene transcription, protein trafficking, and DNA repair. Surprisingly, little is known about the mechanisms by which monoubiquitin signals are produced in the cell. Here, we discuss the potential cellular strategies for generating monoubiquitinated proteins using a few, relatively well characterized examples of monoubiquitinated proteins. These strategies include coupling ubiquitination to low affinity ubiquitin binding, using monoubiquitination-dedicated E2 conjugating enzymes, and restricting ubiquitin chain elongation. Some of these principles may be applicable to protein modifications involving ubiquitin like proteins (UBLs), which often occur in monomeric form.
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