期刊
PROTEOMICS
卷 11, 期 24, 页码 4632-4637出版社
WILEY
DOI: 10.1002/pmic.201100339
关键词
Interaction; Phosphoproteomics; Phosphorylation; Protein kinases; Technology
资金
- NSFC [21021004]
- China State Key Basic Research Program [2012CB910101]
- China High Technology Research Program [2006AA02A309]
- National Key Special Program on Infection diseases [2008ZX10002-017, 2008ZX10002-020]
- MOST [2009IM031800, 2010IM030500]
- DICP
Deciphering the kinasesubstrate relationship is vital for the study of phosphorylation network. The use of immobilized proteins on protein chip as the library for screening of potential kinase substrates is a tried-and-tested method. However, information on phosphorylation sites is lacking and the creation of the library with proteins of whole proteome by recombinant expression is costly and difficult. In this study, a new solid-phase approach by immobilization of proteins from cell lysate onto beads as a protein library for kinase substrate screening was developed. It was found that consensus phosphorylation sites motif for kinase substrates could be accurately determined and hundreds of in vitro kinase substrates and their phosphorylation sites could be identified by using this method.
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