Cancer Institute A national cancer institute
designated cancer center

Matthew Bogyo

Publication Details

  • O-sulfonation of serine and threonine - Mass spectrometric detection and characterization of a new posttranslational modification in diverse proteins throughout the eukaryotes MOLECULAR & CELLULAR PROTEOMICS Medzihradszky, K. F., Darula, Z., Perlson, E., Fainzilber, M., Chalkley, R. J., Ball, H., Greenbaum, D., Bogyo, M., Tyson, D. R., BRADSHAW, R. A., Burlingame, A. L. 2004; 3 (5): 429-440


    Protein sulfonation on serine and threonine residues is described for the first time. This post-translational modification is shown to occur in proteins isolated from organisms representing a broad span of eukaryote evolution, including the invertebrate mollusk Lymnaea stagnalis, the unicellular malaria parasite Plasmodium falciparum, and humans. Detection and structural characterization of this novel post-translational modification was carried out using liquid chromatography coupled to electrospray tandem mass spectrometry on proteins including a neuronal intermediate filament and a myosin light chain from the snail, a cathepsin-C-like enzyme from the parasite, and the cytoplasmic domain of the human orphan receptor tyrosine kinase Ror-2. These findings suggest that sulfonation of serine and threonine may be involved in multiple functions including protein assembly and signal transduction.

    View details for DOI 10.1074/mcp.M300140-MCP200

    View details for Web of Science ID 000221242300001

    View details for PubMedID 14752058

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