Friedrich Miescher Laboratory of the Max Planck Society, Spemannstrasse 39, 72076 Tübingen, Germany.
Eur J Cell Biol. 2010 Feb-Mar;89(2-3):184-93. doi: 10.1016/j.ejcb.2009.11.024. Epub 2010 Jan 12.
Phosphorylation of proteins is a prevalent post-translational modification, which affects intracellular signaling in many ways. About 2% of all eukaryotic genes code for protein kinases catalyzing phosphorylation events. Despite technological advances that have made it possible to identify thousands of phosphorylation sites simultaneously, identification of the substrates of a given kinase remains an exceptionally challenging task. Here, we summarize approaches for substrate identification that make use of genetically engineered 'analog-sensitive' kinases.
蛋白质磷酸化是一种普遍的翻译后修饰方式，它以多种方式影响细胞内信号转导。大约 2%的真核基因编码催化磷酸化事件的蛋白激酶。尽管技术进步使得同时鉴定数千个磷酸化位点成为可能，但鉴定给定激酶的底物仍然是一项极具挑战性的任务。在这里，我们总结了利用基因工程“模拟敏感”激酶进行底物鉴定的方法。
