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Sensitive, Robust, and Cost-Effective Approach for Tyrosine Phosphoproteome Analysis
Dong, Mingming1,2; Bian, Yangyang1,3; Wang, Yan1,2; Dong, Jing1; Yao, Yating1,2; Deng, Zhenzhen1,2; Qin, Hongqiang1; Zou, Hanfa1; Ye, Mingliang1
Source PublicationANALYTICAL CHEMISTRY
2017-09-05
DOI10.1021/acs.analchem.7b02078
Volume89Issue:17Pages:9307-9314
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences
WOS SubjectChemistry, Analytical
WOS Research AreaChemistry
WOS KeywordPHOSPHORYLATION SITES ; SIGNALING PATHWAYS ; SUPERBINDER ; ENRICHMENT ; PROTEOME ; CANCER ; CELLS ; MASS ; EGF
AbstractAlbeit much less abundant than Ser/Thr phosphorylation (pSer/pThr), Tyr phosphorylation (pTyr) is considered as a hallmark in cellular signal transduction. However, its analysis at the proteome level remains challenging. The conventional immunopurification (IP) approach using antibodies specific to pTyr sites is known to have low sensitivity, poor reproducibility and high cost. Our recent study indicated that SH2 domain-derived pTyr-superbinder is a good replacement of pTyr antibody for the specific enrichment of pTyr peptides for phosphoproteomics analysis. In this study, we presented an efficient SH2 superbinder based workflow for the sensitive analysis of tyrosine phosphoproteome. This new method can identify 41% more pTyr peptides than the previous'method. Its excellent performance was demonstrated by the analysis of a variety of different samples. For the highly tyrosine phosphorylated sample, for example, pervanadate-treated Jurkat T cells, it identified over 1800 high confident pTyr sites from only 2 mg of proteins. For the unstimulated Jurkat cells, where the pTyr events rarely occurred, it identified 343 high confident pTyr sites from 5 mg of proteins, which was 31% more than that obtained by the antibody-based method. For the heterogeneous sample of tissue, it identified 197 high confident pTyr sites from 5 mg protein digest of mouse skeletal muscle. In general, it is a sensitive, robust and cost-effective approach and would have wide applications in the study of the regulatory role of tyrosine phosphorylation in diverse physiological and pathological processes.
Language英语
WOS IDWOS:000410014900100
Citation statistics
Cited Times:8[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/149957
Collection中国科学院大连化学物理研究所
Affiliation1.Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&A Ctr, CAS Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Zhengzhou Univ, Affiliated Hosp 1, Med Res Ctr, Zhengzhou 450052, Henan, Peoples R China
Recommended Citation
GB/T 7714
Dong, Mingming,Bian, Yangyang,Wang, Yan,et al. Sensitive, Robust, and Cost-Effective Approach for Tyrosine Phosphoproteome Analysis[J]. ANALYTICAL CHEMISTRY,2017,89(17):9307-9314.
APA Dong, Mingming.,Bian, Yangyang.,Wang, Yan.,Dong, Jing.,Yao, Yating.,...&Ye, Mingliang.(2017).Sensitive, Robust, and Cost-Effective Approach for Tyrosine Phosphoproteome Analysis.ANALYTICAL CHEMISTRY,89(17),9307-9314.
MLA Dong, Mingming,et al."Sensitive, Robust, and Cost-Effective Approach for Tyrosine Phosphoproteome Analysis".ANALYTICAL CHEMISTRY 89.17(2017):9307-9314.
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