PDSM, a motif for phosphorylation-dependent SUMO modification

Ville Hietakangas, Julius Anckar, Henri A Blomster, Mitsuaki Fujimoto, Jorma J Palvimo, Akira Nakai, Lea Sistonen

Research output: Contribution to journalArticleScientificpeer-review


SUMO (small ubiquitin-like modifier) modification regulates many cellular processes, including transcription. Although sumoylation often occurs on specific lysines within the consensus tetrapeptide PsiKxE, 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 (PsiKxExxSP). 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 languageEnglish
Pages (from-to)45-50
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number1
Publication statusPublished - 3 Jan 2006
MoE publication typeA1 Journal article-refereed


  • Amino Acid Motifs/genetics
  • Blotting, Western
  • Consensus Sequence/genetics
  • Electrophoretic Mobility Shift Assay
  • Heat-Shock Proteins/genetics
  • Immunoprecipitation
  • Luciferases
  • Phosphorylation
  • Regulatory Elements, Transcriptional/genetics
  • Reverse Transcriptase Polymerase Chain Reaction
  • Small Ubiquitin-Related Modifier Proteins/metabolism


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