School of Pharmacy, Faculty of Medicine, Health and Life Sciences, Queen's University Belfast, 97 Lisburn Road, Belfast, Northern Ireland BT9 7BL.
Front Biosci (Landmark Ed). 2012 Jan 1;17(3):1184-200. doi: 10.2741/3980.
The conjugation of ubiquitin as either a monomer or as a chain has long been known to regulate the stability, localisation, trafficking and/or function of many intracellular proteins. However, the recent explosion in our knowledge of the enzymes responsible for the removal of ubiquitin suggests they also play an important role in the regulation of many processes. Here we examine what is known about the role of deubiquitinating enzymes (DUBs), with particular emphasis upon their impact on cellular responses to external stimuli. In addition, we look at the evidence that although these enzymes are heavily outnumbered by those responsible for ubiquitin conjugation, that these enzymes may still be important cellular regulators, due to their ability to play multiple roles which can be cell type and cell context specific.
泛素的缀合，无论是单体形式还是链状形式，长期以来一直被认为可以调节许多细胞内蛋白质的稳定性、定位、运输和/或功能。然而，最近我们对负责去除泛素的酶的了解有了爆炸式的增长，这表明它们在许多过程的调节中也起着重要作用。在这里，我们研究了去泛素化酶 (DUBs) 的作用，特别强调了它们对细胞对外界刺激的反应的影响。此外，我们还研究了这样一种证据，尽管这些酶的数量远远少于负责泛素缀合的酶，但由于它们能够发挥多种作用，并且这些作用可能具有细胞类型和细胞环境特异性，因此这些酶仍然可能是重要的细胞调节剂。
