Phosphoproteomics for the Masses

被引:126
作者
Grimsrud, Paul A. [1 ]
Swaney, Danielle L. [1 ]
Wenger, Craig D. [1 ]
Beauchene, Nicole A. [2 ]
Coon, Joshua J. [1 ,2 ]
机构
[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA
[2] Univ Wisconsin, Dept Biomol Chem, Madison, WI 53706 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
Protein phosphorylation; Phosphoproteomics; Shotgun proteomics; Collisional dissociation; Electron-based dissociation; Phosphopeptide enrichment; Isotope labeling; False discovery rate; ELECTRON-TRANSFER DISSOCIATION; EMBRYONIC STEM-CELLS; SITE-SPECIFIC PHOSPHORYLATION; ION AFFINITY-CHROMATOGRAPHY; ISOBARIC TAGGING REAGENTS; PROTEIN-SEQUENCE ANALYSIS; QUANTITATIVE PHOSPHOPROTEOMICS; PHOSPHOPEPTIDE ENRICHMENT; IN-VIVO; SACCHAROMYCES-CEREVISIAE;
D O I
10.1021/cb900277e
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein phosphorylation serves as a primary mechanism of signal transduction in the cells of biological organisms. Technical advancements over the last several years in mass spectrometry now allow for the large-scale identification and quantitation of in vivo phosphorylation at unprecedented levels. These developments have occurred in the areas of sample preparation, instrumentation, quantitative methodology, and informatics so that today, 10 000-20 000 phosphorylation sites can be identified and quantified within a few weeks. With the rapid development and widespread availability of such data, its translation into biological insight and knowledge is a current obstacle. Here we present an overview of how this technology came to be and is currently applied, as well as future challenges for the field.
引用
收藏
页码:105 / 119
页数:15
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