O-sulfonation of serine and threonine

K. F. Medzihradszky, Z. Darula, E. Perlson, M. Fainzilber, R. J. Chalkley, H. Ball, D. Greenbaum, M. Bogyo, D. R. Tyson, R. A. Bradshaw, A. L. Burlingame*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)429-443
Number of pages15
JournalMolecular and Cellular Proteomics
Issue number5
StatePublished - May 2004
Externally publishedYes


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