PDSM, a motif for phosphorylation-dependent SUMO modification

V Hietakangas, J Anckar, HA Blomster, M Fujimoto, JJ Palvimo, A Nakai, Lea Sistonen

    Research output: Contribution to journalArticleScientificpeer-review

    350 Citations (Scopus)

    Abstract

    SUMO (small ubiquitin-like modifier) modification regulates many cellular processes, including transcription. Although sumoylation often occurs on specific lysines within the consensus tetrapeptide Psi KxE, other modifications, such as phosphorylation, may regulate the sumoylation of a substrate. We have discovered PDSM (phosphorylation-dependent sumoylation motif), composed of a SUMO consensus site and an adjacent proline-directed phosphorylation site (Psi KxExxSP). The highly conserved motif regulates phosphorylation-dependent sumoylation of multiple substrates, such as heat-shock factors (HSFs), GATA-1, and myocyte enhancer factor 2. In fact, the majority of the PDSM-containing proteins are transcriptional regulators. Within the HSF family, PDSM is conserved between two functionally distinct members, HSF1 and HSF4b, whose transactivation capacities are repressed through the phosphorylation-dependent sumoylation. As the first recurrent sumoylation determinant beyond the consensus tetrapeptide, the PDSM provides a valuable tool in predicting new SUMO substrates.
    Original languageUndefined/Unknown
    Pages (from-to)45–50
    Number of pages6
    JournalProceedings of the National Academy of Sciences
    Volume103
    Issue number1
    Publication statusPublished - 2006
    MoE publication typeA1 Journal article-refereed

    Keywords

    • heat-shock factor
    • heat-shock protein
    • transcription

    Cite this