Abstract：
: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.
journal_name
J Proteome Resjournal_title
Journal of proteome researchauthors
Zhang G,Neubert TAdoi
10.1021/pr200697xsubject
Has Abstractpub_date
2011-12-02 00:00:00pages
5454-62issue
12eissn
1535-3893issn
1535-3907journal_volume
10pub_type
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journal_title：Journal of proteome research
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更新日期：2012-06-01 00:00:00
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journal_title：Journal of proteome research
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journal_title：Journal of proteome research
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更新日期：2017-11-03 00:00:00
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journal_title：Journal of proteome research
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更新日期：2013-12-06 00:00:00
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journal_title：Journal of proteome research
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更新日期：2009-02-01 00:00:00
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