Absolute Phosphorylation Stoichiometry Analysis by Motif-Targeting Quantitative Mass Spectrometry
Absolute Phosphorylation Stoichiometry Analysis by Motif-Targeting Quantitative Mass Spectrometry
复制标题
通过基序靶向定量质谱法进行绝对磷酸化化学计量分析
DOI：
10.1007/978-1-4939-7154-1_20
复制
发表时间：
2017
影响因子：
--
通讯作者：
Ishihama Yasushi
中科院分区：
文献类型：
--
作者：
Tsai Chia-Feng;Ku Wei-Chi;Chen Yu-Ju;Ishihama Yasushi
位点特异性磷酸化化学计量的直接测量可以明确地区分磷酸化程度是由上游激酶/磷酸酶活性调节还是由转录调节来改变蛋白质表达水平。在这里，我们描述了一种靶向基序的定量蛋白质组学方法，该方法集成了去磷酸化、同位素标签标记和酶促激酶反应，用于人类蛋白质组的大规模磷酸化化学计量测量。
Direct measurement of site-specific phosphorylation stoichiometry can unambiguously distinguish whether the degree of phosphorylation is regulated by upstream kinase/phosphatase activity or by transcriptional regulation to alter protein expression level. Here, we describe a motif-targeting quantitative proteomic approach that integrates dephosphorylation, isotope tag labeling, and enzymatic kinase reaction for large-scale phosphorylation stoichiometry measurement of the human proteome.