期刊
JOURNAL OF PROTEOME RESEARCH
卷 10, 期 12, 页码 5454-5462出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr200697x
关键词
phosphoproteomic; RTK; titanium dioxide; EphB; quantitation; phosphorylation; phosphopeptide; SILAC; mass spectrometry; proteomics
资金
- National Institutes of Health [P30 NS050276, S10 RR 017990-01]
- NCI [2P30 CA 016087]
There are three quantitative phosphoproteomic strategies most commonly used to study receptor tyrosine kinase (RTK) signaling. These strategies quantify changes in: (1) all three forms of phosphosites (phosphoserine, phosphothreonine and phosphotyrosine) following enrichment of phosphopeptides by titanium dioxide or immobilized metal affinity chromatography; (2) phosphotyrosine sites following anti- phosphotyrosine antibody enrichment of phosphotyrosine peptides; or (3) phosphotyrosine proteins and their binding partners following anti-phosphotyrosine protein immunoprecipitation. However, it is not clear from literature which strategy is more effective. In this study, we assessed the utility of these three phosphoproteomic strategies in RTK signaling studies by using EphB receptor signaling as an example. We used all three strategies with stable isotope labeling with amino acids in cell culture (SILAC) to compare changes in phosphoproteomes upon EphB receptor activation. We used bioinformatic analysis to compare results from the three analyses. Our results show that the three strategies provide complementary information about RTK pathways.
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