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Protein phosphorylation has emerged as a ubiquitous regulatory switch in cell signaling networks. Improved methods to purify and characterize phosphopeptides have led to an explosion of phosphorylation site data, and we can now explore how protein phosphorylation evolved. This question has been tackled by two studies in this issue. On page 1686, Tan et al. (1) report that tyrosine residues (which can be phosphorylated) have been selectively lost through metazoan evolution. On page 1682, Holt et al. (2) show that most phosphorylation sites shift position in rapidly evolving, disordered regions of proteins.
Proteomic Mass Spectrometry Group, The Wellcome Trust Sanger Institute, Hinxton, Cambridge CB10 1SA, UK.
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