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Genome Biology volume 4, Article number: spotlight-20030221-01 (2003)
Protein phosphorylation on serine, threonine or tyrosine residues, can regulate protein-protein interactions via specific binding to the phospho-residues. In the February 21 Science Elia et al. describe a proteomic screen designed to isolate novel phospho-binding proteins (Science 2003, 299:1228-1231). The technique involves the creation of a library of biased partially degenerate phosphopeptides that are immobilized and used as a 'bait' in a screen for binding proteins. Elia et al. tested the technique with peptides resembling substrates of cyclin-dependent kinase and isolated the mitotic kinase Plk1 (polo-like kinase 1). The phospho-binding domain of Plk1 is important for localisation to the centrosome during mitosis. Elia et al. identified the phosphopeptide-binding domain and tested binding specificities, providing important proof-of-principle for their approach.
Protein-protein interactions define specificity in signal transduction.
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Weitzman, J.B. Phosphopeptide proteomics. Genome Biol 4, spotlight-20030221-01 (2003). https://doi.org/10.1186/gb-spotlight-20030221-01
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