PDSM, a motif for phosphorylation-dependent SUMO modification

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Hietakangas V, Anckar J, Blomster HA, Fujimoto M, Palvimo JJ, Nakai A, Sistonen L
Publisher: NATL ACAD SCIENCES
Publication year: 2006
Journal: Proceedings of the National Academy of Sciences
Journal acronym: P NATL ACAD SCI USA
Volume number: 103
Issue number: 1
Start page: 45
End page: 50
Number of pages: 6
ISSN: 0027-8424
eISSN: 1091-6490


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.


Keywords

heat-shock factor, heat-shock protein, transcription

Last updated on 2019-21-04 at 05:30