Global, quantitative and dynamic mapping of protein subcellular localization
Global, quantitative and dynamic mapping of protein subcellular localization
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DOI：
10.7554/elife.16950
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发表时间：
2016-06-09
期刊：
影响因子：
7.7
通讯作者：
Borner, Georg H. H.
中科院分区：
文献类型：
--
作者：
Itzhak, Daniel N.;Tyanova, Stefka;Borner, Georg H. H.
亚细胞定位对蛋白质功能有重要影响，细胞通过控制蛋白质定位来调节生物学过程。我们已经开发并应用了动态细胞器图谱，这是一种蛋白质组学方法，可以对蛋白质易位事件进行全局映射。我们最初静态地使用地图来生成一个数据库，该数据库具有来自HeLa细胞的超过8700种蛋白质的定位和绝对拷贝数信息，接近全面覆盖。所有主要的细胞器都得到了解析，预测准确度非常高（估计>92%）。结合空间和丰度信息，在蛋白质水平上对HeLa细胞的解剖结构和细胞器组成进行了前所未有的定量研究。随后，我们通过捕获EGF刺激后的易位事件来证明该方法的动态能力，并将其整合到定量模型中。动态细胞器图谱能够对生理蛋白质运动进行蛋白质组范围的分析，而不需要任何特定于所研究过程的试剂，因此将广泛应用于细胞生物学。
Subcellular localization critically influences protein function, and cells control protein localization to regulate biological processes. We have developed and applied Dynamic Organellar Maps, a proteomic method that allows global mapping of protein translocation events. We initially used maps statically to generate a database with localization and absolute copy number information for over 8700 proteins from HeLa cells, approaching comprehensive coverage. All major organelles were resolved, with exceptional prediction accuracy (estimated at >92%). Combining spatial and abundance information yielded an unprecedented quantitative view of HeLa cell anatomy and organellar composition, at the protein level. We subsequently demonstrated the dynamic capabilities of the approach by capturing translocation events following EGF stimulation, which we integrated into a quantitative model. Dynamic Organellar Maps enable the proteome-wide analysis of physiological protein movements, without requiring any reagents specific to the investigated process, and will thus be widely applicable in cell biology.