An extended consensus motif enhances the specificity of substrate modification by SUMO

Shen Hsi Yang, Alex Galanis, James Witty, Andrew D. Sharrocks

    Research output: Contribution to journalArticlepeer-review


    Protein modification by SUMO conjugation is an important regulatory event. Sumoylation usually takes place on a lysine residue embedded in the core consensus motif ψKxE. However, this motif confers limited specificity on the sumoylation process. Here, we have probed the roles of clusters of acidic residues located downstream from the core SUMO modification sites in proteins such as the transcription factor Elk-1. We demonstrate that these are functionally important in SUMO-dependent transcriptional repression of Elk-1 transcriptional activity. Mechanistically, the acidic residues are important in enhancing the efficiency of Elk-1 sumoylation by Ubc9. Similar mechanisms operate in other transcription factors and phosphorylation sites can functionally substitute for acidic residues. Thus, an extended sumoylation motif, termed the NDSM (negatively charged amino acid-dependent sumoylation motif), helps define functional SUMO targets. We demonstrate that this extended motif can be used to correctly predict novel targets for SUMO modification. © 2006 European Molecular Biology Organization. All Rights Reserved.
    Original languageEnglish
    Pages (from-to)5083-5093
    Number of pages10
    JournalEMBO Journal
    Issue number21
    Publication statusPublished - 1 Nov 2006


    • Elk-1
    • SUMO
    • Transcription repression
    • Ubc9


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