Systematic study of the dynamics and half-lives of newly synthesized proteins in human cells.
Systematic study of the dynamics and half-lives of newly synthesized proteins in human cells.
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DOI：
10.1039/c5sc03826j
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发表时间：
2016-02-01
期刊：
影响因子：
8.4
通讯作者：
Wu R
中科院分区：
文献类型：
--
作者：
Chen W;Smeekens JM;Wu R
开发了一种新的化学蛋白质组学方法来特异性地鉴定新合成的蛋白质并测量其半衰期。蛋白质动力学在调节几乎每一个细胞事件中是必不可少的，并且异常的蛋白质稳态是许多疾病的根源。要在全球范围内研究蛋白质动力学并准确测量其半衰期是非常困难的。在这里，我们已经开发了一种化学蛋白质组学方法集成蛋白质标记，点击化学和多重蛋白质组学，克服了现有方法的挑战。用叠氮基高丙氨酸（AHA）和重赖氨酸标记使我们能够选择性地富集新合成的蛋白质，将它们与现有的蛋白质明确区分开来，并减少重氨基酸循环的影响。此外，多重蛋白质组学使我们能够同时在多个时间点定量蛋白质，从而提高测量蛋白质丰度变化及其半衰期的准确性。对新合成蛋白质动力学的系统研究将为蛋白质稳态和疾病的分子机制提供深入了解。
A novel chemical proteomics method was developed to specifically identify newly synthesized proteins and measure their half-lives. Protein dynamics are essential in regulating nearly every cellular event, and aberrant proteostasis is the source of many diseases. It is extraordinarily difficult to globally study protein dynamics and accurately measure their half-lives. Here we have developed a chemical proteomics method integrating protein labeling, click chemistry and multiplexed proteomics, which overcomes current challenges with existing methods. Labeling with both azidohomoalanine (AHA) and heavy lysine allows us to selectively enrich newly synthesized proteins, clearly distinguish them from existing proteins, and reduce the impact of heavy amino acid recycling. Moreover, multiplexed proteomics enables us to quantify proteins at multiple time points simultaneously, thus increasing the accuracy of measuring protein abundance changes and their half-lives. Systematic investigation of newly synthesized protein dynamics will provide insight into proteostasis and the molecular mechanisms of disease.
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影响因子：
4.9
作者：
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通讯作者：
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影响因子：
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DOI：
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发表时间：
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