Xu Yangfan, Fan Xianqun, Hu Yang
Department of Ophthalmology, Stanford University School of Medicine, Palo Alto, CA, 94304, USA.
Department of Ophthalmology, Ninth People's Hospital, Shanghai JiaoTong University School of Medicine, Shanghai, People's Republic of China.
Cell Biosci. 2021 Jan 29;11(1):27. doi: 10.1186/s13578-021-00542-3.
Enzyme-catalyzed proximity labeling (PL) combined with mass spectrometry (MS) has emerged as a revolutionary approach to reveal the protein-protein interaction networks, dissect complex biological processes, and characterize the subcellular proteome in a more physiological setting than before. The enzymatic tags are being upgraded to improve temporal and spatial resolution and obtain faster catalytic dynamics and higher catalytic efficiency. In vivo application of PL integrated with other state of the art techniques has recently been adapted in live animals and plants, allowing questions to be addressed that were previously inaccessible. It is timely to summarize the current state of PL-dependent interactome studies and their potential applications. We will focus on in vivo uses of newer versions of PL and highlight critical considerations for successful in vivo PL experiments that will provide novel insights into the protein interactome in the context of human diseases.
酶催化邻近标记(PL)与质谱(MS)相结合,已成为一种革命性的方法,用于揭示蛋白质-蛋白质相互作用网络、剖析复杂的生物过程,并在比以往更接近生理状态的条件下对亚细胞蛋白质组进行表征。酶标签正在不断升级,以提高时间和空间分辨率,并获得更快的催化动力学和更高的催化效率。最近,PL与其他先进技术相结合的体内应用已在活体动物和植物中得到应用,使得以前无法解决的问题得以解决。及时总结PL依赖的相互作用组研究的现状及其潜在应用是很有必要的。我们将重点关注新版本PL在体内的应用,并强调成功进行体内PL实验的关键注意事项,这些实验将为人类疾病背景下的蛋白质相互作用组提供新的见解。