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Phosphopeptide proteomics

Jonathan B Weitzman

Author Affiliations

Genome Biology 2003, 4:spotlight-20030221-01  doi:10.1186/gb-spotlight-20030221-01

The electronic version of this article is the complete one and can be found online at:


Published:21 February 2003

© 2003 BioMed Central Ltd

Research news

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.

References

  1. Protein-protein interactions define specificity in signal transduction.

    PubMed Abstract | Publisher Full Text OpenURL

  2. [http://www.sciencemag.org] webcite

    Science