PDSM, a motif for phosphorylation-dependent SUMO modification

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

Tutkimustuotos: LehtiartikkeliArtikkeliTieteellinenvertaisarvioitu

Abstrakti

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.

AlkuperäiskieliEnglanti
Sivut45-50
Sivumäärä6
JulkaisuProceedings of the National Academy of Sciences of the United States of America
Vuosikerta103
Numero1
DOI - pysyväislinkit
TilaJulkaistu - 3 tammik. 2006
OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu

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