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Sci. Signal., 6 December 2011
Vol. 4, Issue 202, p. ra83
[DOI: 10.1126/scisignal.2002105]


Editor's Summary

Building Complexity with Phosphotyrosine
Regulated protein-protein interactions are crucial to cellular signal transduction. SH2 domains recognize specific sequences containing phosphorylated tyrosine residues. Signaling through tyrosine phosphorylation networks has expanded as organisms have become more complex. Liu et al. combined sequence alignment, analysis of intron and exon boundaries, and domain organization of 21 living species, ranging from amoeba and slime mold to humans, to classify the hundreds of known SH2 domain–containing proteins into 38 families. Their analysis suggests mechanisms by which SH2 and tyrosine kinase signaling networks have evolved and contributed to the development of organismal complexity.

Citation: B. A. Liu, E. Shah, K. Jablonowski, A. Stergachis, B. Engelmann, P. D. Nash, The SH2 Domain–Containing Proteins in 21 Species Establish the Provenance and Scope of Phosphotyrosine Signaling in Eukaryotes. Sci. Signal. 4, ra83 (2011).

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