POLYSUMOYLATION-MEDIATED RELOCALISATION OF PROTEINS TO THE NUCLEUS
Protein modification with the small ubiquitin-related modifier (SUMO) is an essential reversible regulatory mechanism in eukaryotic cells known to cross-talk to other PTMs such as ubiquitylation, phosphorylation, and acetylation. Fluorescent reporter proteins fused to SUMO chains are strongly enriched in the cell nucleus. The goal of this project is to elucidate the mechanism of polysumoylation-mediated nuclear translocation and to investigate its reversibility.
Pabst, S., L.M. Döring, N. Petreska, R.J. Dohmen (2019), Methods to study SUMO dynamics in yeast. Methods Enzymol. 618: p. 187-210.
Eckhoff, J. and R.J. Dohmen (2015), In Vitro Studies Reveal a Sequential Mode of Chain Processing by the Yeast SUMO (Small Ubiquitin-related Modifier)-specific Protease Ulp2. J Biol Chem. 290(19): p. 12268-81.
- Sriramachandran, A.M., and R.J. Dohmen (2014), SUMO-targeted ubiquitin ligases. Biochim Biophys Acta.1843(1): p. 75-85.