PDSM, a motif for phosphorylation-dependent SUMO modification

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

    Forskningsoutput: TidskriftsbidragArtikelVetenskapligPeer review

    350 Citeringar (Scopus)

    Sammanfattning

    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.
    OriginalspråkOdefinierat/okänt
    Sidor (från-till)45–50
    Antal sidor6
    TidskriftProceedings of the National Academy of Sciences
    Volym103
    Utgåva1
    StatusPublicerad - 2006
    MoE-publikationstypA1 Tidskriftsartikel-refererad

    Nyckelord

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

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