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. 2007 Jun 22;26(6):899-915.
doi: 10.1016/j.molcel.2007.05.031.

High-throughput phosphotyrosine profiling using SH2 domains

Kazuya Machida  1 , Christopher M Thompson, Kevin Dierck, Karl Jablonowski, Satu Kärkkäinen, Bernard Liu, Haimin Zhang, Piers D Nash, Debra K Newman, Peter Nollau, Tony Pawson, G Herma Renkema, Kalle Saksela, Martin R Schiller, Dong-Guk Shin, Bruce J Mayer
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Free article

High-throughput phosphotyrosine profiling using SH2 domains

Kazuya Machida et al. Mol Cell. .
Free article

Abstract

Protein tyrosine phosphorylation controls many aspects of signaling in multicellular organisms. One of the major consequences of tyrosine phosphorylation is the creation of binding sites for proteins containing Src homology 2 (SH2) domains. To profile the global tyrosine phosphorylation state of the cell, we have developed proteomic binding assays encompassing nearly the full complement of human SH2 domains. Here we provide a global view of SH2 domain binding to cellular proteins based on large-scale far-western analyses. We also use reverse-phase protein arrays to generate comprehensive, quantitative SH2 binding profiles for phosphopeptides, recombinant proteins, and entire proteomes. As an example, we profiled the adhesion-dependent SH2 binding interactions in fibroblasts and identified specific focal adhesion complex proteins whose tyrosine phosphorylation and binding to SH2 domains are modulated by adhesion. These results demonstrate that high-throughput comprehensive SH2 profiling provides valuable mechanistic insights into tyrosine kinase signaling pathways.

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