摘要
蛋白质磷酸化修饰是调控多样种生物过程的一种重要的翻译后修饰,定量分析内部和外部因子作用下磷酸化蛋白质的分子调控机制对理解生物功能非常重要。早期磷酸化蛋白质组研究的重点是定性检测、鉴定磷酸化蛋白质及磷酸化位点的定位。近年来,随着质谱技术的快速发展使得定量磷酸化蛋白质组研究有了很大的发展。利用磷酸化蛋白质组的定量分析监测蛋白质磷酸化的动态变化有助于阐明生物过程及其功能的实现机制。本文综述了磷酸化蛋白质组定量分析策略:基于2-DE的磷酸化蛋白质组定量策略,基于无胶的质谱磷酸化蛋白质组标记定量策略及无标记定量分析策略。磷酸化蛋白质组的定量分析将有助于更好的阐明生物的信号传导机制。
Protein phosphorylation is an important post-translational modification in organisms for the regulation of diverse biological processes. Quantitative analysis of the phosphorylated proteins is important for understanding the biological functions under internal and external factors. The early studies focus on the qualitative analysis, identification and location of protein phosphorylation sites. In recent years, with the rapid development of mass spectrometry, the quantitative analysis strategies on phosphoproteomics have been made great progress. Monitoring changes in phosphorylated proteins is capable of clarifying the processes of biological functions. In this paper, we mainly present an overview of several strategies of quantitative phosphoproteomics, such as strategies of quantitative phosphoproteomics based on 2-DE, quantitative phosphoproteomics based on gel-free MS/MS labelling and label free, etc. Quantitative analysis of protein phosphorylation would be help to better elucidate the signal transduction mechanisms of biological processes.
出处
《分子植物育种》
CAS
CSCD
北大核心
2014年第3期577-583,共7页
Molecular Plant Breeding
基金
江苏省高校自然科学重大研究项目(12KJA220002)
博士点基金优先发展领域(20113204130002)
江苏省政府优势学科(林学)建设项目(PAPD)共同资助
关键词
翻译后修饰
磷酸化蛋白质组
质谱
双向电泳
Post-translational modification, Phosphoproteomics, Mass spectrometry, 2-DE
