基于蛋白质的荧光传感器在体内检测N-乙酰半乳糖胺转移酶的活性
Activity Detection of GalNAc Transferases by Protein-Based Fluorescence Sensors In Vivo.
作者信息
Song Lina, Bachert Collin, Linstedt Adam D
机构信息
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA, 15213, USA.
出版信息
Methods Mol Biol. 2016;1496:123-31. doi: 10.1007/978-1-4939-6463-5_10.
Abstract
Mucin-type O-glycosylation occurring in the Golgi apparatus is an important protein posttranslational modification initiated by up to 20 GalNAc-transferase isozymes with largely distinct substrate specificities. Regulation of this enzyme family affects a vast array of proteins transiting the secretory pathway and misregulation causes human diseases. Here we describe the use of protein-based fluorescence sensors that traffic in the secretory pathway to monitor GalNAc-transferase activity in living cells. The sensors can either be "pan" or isozyme specific.
摘要
发生在高尔基体中的粘蛋白型O-糖基化是一种重要的蛋白质翻译后修饰，由多达20种具有不同底物特异性的N-乙酰半乳糖胺转移酶同工酶启动。该酶家族的调控影响大量通过分泌途径的蛋白质，调控异常会导致人类疾病。在这里，我们描述了使用在分泌途径中运输的基于蛋白质的荧光传感器来监测活细胞中N-乙酰半乳糖胺转移酶的活性。这些传感器可以是“泛”型的，也可以是同工酶特异性的。
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