Mimnaugh E G, Bonvini P, Neckers L
Tumor Cell Biology Section, Medicine Branch, National Cancer Institute, National Institutes of Health, Key West Center, Rockville, MD 20850, USA.
Electrophoresis. 1999 Feb;20(2):418-28. doi: 10.1002/(SICI)1522-2683(19990201)20:2<418::AID-ELPS418>3.0.CO;2-N.
Ubiquitination of key cellular proteins involved in signal transduction, gene transcription and cell-cycle regulation usually condemns those proteins to proteasomal or lysosomal degradation. Additionally, cycles of reversible ubiquitination regulate the function of certain proteins in a manner analogous to phosphorylation. In this short review we describe the current methodology for measuring ubiquitin and ubiquitination, provide examples which illustrate how various techniques have been used to study protein ubiquination, alert the readers of pitfalls to avoid, and offer guidelines to investigators newly interested in this novel post-translational protein modification.
参与信号转导、基因转录和细胞周期调控的关键细胞蛋白的泛素化通常会导致这些蛋白被蛋白酶体或溶酶体降解。此外，可逆泛素化循环以类似于磷酸化的方式调节某些蛋白的功能。在这篇简短的综述中，我们描述了目前测量泛素和泛素化的方法，提供了一些例子来说明各种技术是如何用于研究蛋白质泛素化的，提醒读者避免陷阱，并为刚对这种新型蛋白质翻译后修饰感兴趣的研究人员提供指导。
