Postgenomic Technology Group, Institute of Applied and Fundamental Medicine, Nizhny Novgorod State Medical Academy, Nizhny Novgorod, 603005, Russia.
Sci Signal. 2013 Jun 18;6(280):pe22. doi: 10.1126/scisignal.2004251.
Ubiquitylation, a widespread and important posttranslational modification of eukaryotic proteins, regulates a multitude of critical cellular processes, both in normal and pathological conditions. A classical view of how ubiquitylation regulates protein function involves recognition of ubiquitin-encoded signals by specific ubiquitin-binding domains. However, evidence suggests the existence of direct effects of ubiquitylation, which occur through its impact on protein-protein interactions that do not involve specific ubiquitin receptors. Ubiquitin attachment may cause steric limitations that influence interaction of the modified protein with other proteins. Here, we present examples of this direct effect of ubiquitylation and propose how a two-level ubiquitin-mediated regulatory mechanism may provide flexibility.
泛素化是真核生物蛋白中广泛而重要的一种翻译后修饰，它调节着许多关键的细胞过程，无论是在正常还是病理条件下。泛素化如何调节蛋白质功能的经典观点涉及到特定泛素结合结构域对泛素编码信号的识别。然而，有证据表明泛素化存在直接影响，这种影响是通过其对不涉及特定泛素受体的蛋白质-蛋白质相互作用的影响来实现的。泛素的附着可能会引起空间限制，从而影响修饰蛋白与其他蛋白的相互作用。在这里，我们提出了泛素化这种直接作用的例子，并提出了一种两级泛素介导的调节机制如何提供灵活性的想法。
