Shenoy Sudha K
Duke University Medical Center, Departments of Medicine and Cell Biology, Durham, NC 27710, USA.
Circ Res. 2007 Apr 27;100(8):1142-54. doi: 10.1161/01.RES.0000261939.88744.5a.
Regulation of protein function by posttranslational modification plays an important role in many biological pathways. The most well known among such modifications is protein phosphorylation performed by highly specific protein kinases. In the past decade, however, covalent linkage of the low-molecular-weight protein ubiquitin to substrate proteins (protein ubiquitination) has proven to be yet another widely used mechanism of protein regulation playing a crucial role in virtually all aspects of cellular functions. This review highlights some of the recently discovered and provocative roles for ubiquitination in the regulation of the life cycle and signal transduction properties of 7-transmembrane receptors that serve to integrate many biological functions and play fundamental roles in cardiovascular homeostasis.
翻译后修饰对蛋白质功能的调节在许多生物途径中起着重要作用。这类修饰中最广为人知的是由高度特异性蛋白激酶进行的蛋白质磷酸化。然而,在过去十年中,低分子量蛋白质泛素与底物蛋白的共价连接(蛋白质泛素化)已被证明是另一种广泛使用的蛋白质调节机制,几乎在细胞功能的所有方面都起着关键作用。本综述重点介绍了泛素化在7跨膜受体的生命周期调节和信号转导特性方面最近发现的一些具有启发性的作用,这些受体整合了许多生物学功能,并在心血管稳态中发挥着重要作用。