Abstract:
:Deciphering global signaling networks is of great importance for the detailed understanding of cellular signaling processes controlling many important biological functions. Among signaling processes, tyrosine phosphorylation has a central role. At present, adequate techniques for the global characterization of the tyrosine phosphoproteome are lacking, particularly for the analysis of small amounts of protein. By combining the power of PCR amplification with the unique properties of Src homology region 2 (SH2) domains to specifically recognize tyrosine-phosphorylated proteins, we developed a new proteomic approach, termed oligonucleotide-tagged multiplex assay (OTM). For OTM, multiple SH2 domains are labeled by domain-specific oligonucleotide tags, applied as probes to complex protein mixtures in a multiplex reaction and phosphotyrosine-specific interactions are quantified by PCR. Using OTM we reproducibly quantified differential states of tyrosine phosphorylation with high sensitivity and specificity in small amounts of whole cellular extracts as demonstrated for various tumor cell lines and human leukemia samples.
journal_name
Nat Methodsjournal_title
Nature methodsauthors
Dierck K,Machida K,Voigt A,Thimm J,Horstmann M,Fiedler W,Mayer BJ,Nollau Pdoi
10.1038/nmeth917subject
Has Abstractpub_date
2006-09-01 00:00:00pages
737-44issue
9eissn
1548-7091issn
1548-7105pii
nmeth917journal_volume
3pub_type
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