A02 | Role of SUMO and ubiquitin modifications in the control of mitochondrial fission
Running time within the CRC 1218: 07/2016 - 06/2020
Mitochondria form a highly dynamic intracellular network, which is regulated by fusion and fission events. In this project, we will investigate the role of sumoylation and ubiquitylation in the regulation of mitochondrial fission. The long-term goal of this project is to understand the regulation of mitochondrial fission in response to physiological needs by a cross talk of SUMO and ubiquitin modifications.
Sriramachandran, A.M., Meyer-Teschendorf, K., Pabst, S., Ulrich, H.D., Gehring, N.H., Hofmann, K., Praefcke, G.J.K. Dohmen, and R.J. (2019). Arkadia/RNF111 is a SUMO-targeted ubiquitin ligase with preference for substrates marked with SUMO1-capped SUMO2/3 chain. Nat. Comm. doi.org/10.1038/s41467-019-11549-3. [Epub ahead of print]
Schuster, R., Anton, V., Simoes, T., Altin, S., den Brave, F., Hermanns, T., Hospenthal, M., Komander, D., Dittmar, G., Dohmen, R.J., Escobar-Henriques, M. (2019). Dual role of a GTPase conformational switch for membrane fusion by mitofusin ubiquitylation. Life Sci. Alliance, 3(1). pii: e201900476. doi: 10.26508/lsa.201900476. Print 2020 Jan.
Pabst, S., Döring, L.M., Petreska, N., Dohmen. R.J. (2019). Methods to study SUMO dynamics in yeast. Methods Enzymol. 618, 187-210.
Eckhoff, J. and Dohmen, R.J. (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, 12268-12281.