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B03 - Regulation of mitochondrial surveillance by the UPS

Thorsten Hoppe
CECAD Research Center/Institute for Genetics
University of Cologne

E-mail: Thorsten.HoppeSpamProtectionuni-koeln.de
Phone: +49 - 221 / 478 84218
For more information and contact please visit the HOPPE LAB.

Caenorhabditis elegans mutants with increased levels of reactive oxygen species (ROS) are limited in protein turnover, demonstrating that mitochondrial stress affects the ubiquitin/proteasome system (UPS). Intriguingly, related disease-causing mutations associated with mitochondrial failure provide similar proteolytic defects in humans. The central objective of our proposed research is to identify conserved mechanisms that coordinate mitochondrial metabolism and ubiquitin-dependent proteostasis in the context of cellular and organismal physiology.

Latest publications
Franz, A., Ackermann, L. and Hoppe, T.  (2016). Ring of change: CDC48/p97 drives protein dynamics at chromatin. Front. Genet. 7, 73.

Franz, A., Kevei, É., and Hoppe, T. (2015). Double-edged alliance: mitochondrial surveillance by the UPS and autophagy. Curr. Opin. Cell Biol. 4, 37:18-27.

Segref, A., Kevei, É., Pokrzywa, W., Schmeisser, K., Mansfeld, J., Livnat-Levanon, N., Ensenauer, R., Glickman, M.H., Ristow, M., and Hoppe, T. (2014). Pathogenesis of human mitochondrial diseases is modulated by reduced activity of the ubiquitin/proteasome system. Cell Metab.  19, 642-652.

Livnat-Levanon, N., Kevei, É., Kleifeld, O., Krutauz, D., Segref, A., Rinaldi, T., Erpapazoglou, Z., Cohen, M., Reis, N., Hoppe, T., Glickman M.H. (2014). Reversible 26S Proteasome disassembly upon mitochondrial stress. Cell Rep.  7, 1371-1380.