Gao Min, Karin Michael
Pharmacopeia Drug Discovery, Cranbury, New Jersey 08512, USA.
Mol Cell. 2005 Sep 2;19(5):581-93. doi: 10.1016/j.molcel.2005.08.017.
Like many other posttranscriptional modifications, ubiquitination and conjugation of ubiquitin-like polypeptides to target proteins are tightly regulated by extracellular stimuli. In many cases, this regulation is dependent upon protein phosphorylation. The regulatory step affected by phosphorylation could involve either recognition of the substrate by an E3 ubiquitin ligase or the actual conjugation reaction. Regulation occurs through phosphorylation of either the substrates or the E3 ligases themselves. This review focuses on recent advances in understanding how extracellular stimuli modulate the attachment of ubiquitin and ubiquitin-like peptides to target proteins.
与许多其他转录后修饰一样，泛素化以及泛素样多肽与靶蛋白的缀合受到细胞外刺激的严格调控。在许多情况下，这种调控依赖于蛋白质磷酸化。受磷酸化影响的调控步骤可能涉及E3泛素连接酶对底物的识别或实际的缀合反应。调控通过底物或E3连接酶自身的磷酸化来实现。本综述着重介绍了在理解细胞外刺激如何调节泛素和泛素样肽与靶蛋白的附着方面的最新进展。
