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B02 | Mitochondrial hydrogen peroxide signaling

Jan Riemer
Institute for Biochemistry
University of Cologne

E-mail: jan.riemerSpamProtectionuni-koeln.de
Phone: +49 - 221 / 470 7306
For more information and contact please visit the RIEMER LAB.


Running time within the CRC 1218: 07/2016 - 06/2024.
 

Abstract

Hydrogen peroxide (H2O2) is an unavoidable byproduct of aerobic life. It can be beneficial and deleterious depending on its levels and fluxes, and the functional state of the cell. We will investigate H2O2 handling in human cells, its release to the cytosol, the control of release by different mitochondrial and extra-mitochondrial systems and the impact of mitochondrial H2O2 on physiological processes and cellular proteins. Collectively, we will with this project in mammalian cells answer fundamental questions on the where, when and how of mitochondrial H2O2 production and on the role of H2O2 in coordinating mitochondrial function with the rest of the cell.

Project-related publications

Calabrese, G., Peker, E., Amponsah, P.S., Hoehne, M.N., Riemer, T., Mai, M., Bienert, G.P., Deponte, M., Morgan, B., and Riemer, J. (2019). Hyperoxidation of mitochondrial peroxiredoxin limits H2O2-induced cell death in yeast. EMBO J. e101552. doi.org/10.15252/embj.2019101552. [Epub ahead of print]

Habich, M., Salscheider, S.L., Murschall, L.M., Hoehne, M.N., Fischer, M., Schorn, F., Petrungaro, C., Ali, M., Erdogan, A.J., Abou-Eid, S., Kashkar, H., Dengjel, J., and Riemer, J. (2019). Vectorial import via a metastable disulfide-linked complex allows for a quality control step and import by the mitochondrial disulfide relay. Cell Rep. 26, 759-774.

Anton, V., Buntenbroich, I., Schuster, R., Babatz, F., Simões, T., Altin, S., Calabrese, G., Riemer, J., Schauss, A., and Escobar-Henriques, M. (2019). Plasticity in salt-bridge allows fusion-competent ubiquity-lation of mitofusins and Cdc48 recognition. Life Sci. Alliance 2, 2(6). doi: 10.26508/lsa.201900491.

MacVicar, T., Ohba, Y., Nolte, H., Mayer, F.C., Tatsuta, T., Sprenger, H.G., Lindner, B., Zhao, Y., Li, J., Bruns, C., Krüger, M., Habich, M., Riemer, J., Schwarzer, R., Pasparakis, M., Henschke, S., Brüning, J.C., Zamboni, N., and Langer, T. (2019). Lipid signalling drives proteolytic rewiring of mitochondria by YME1L. Nature 575, 361-365.

Roma, L.P., Deponte, M., Riemer, J., and Morgan, B. (2018). Mechanisms and applications of redox-sensitive green fluorescent protein-based hydrogen peroxide probes. Antioxid. Redox Signaling 29, 552-568.

Habich, M., Salscheider, S.L., and Riemer, J. (2018). Cysteine residues in mitochondrial intermembrane space proteins: more than just import. Br. J. Pharmacol. 176, 514-531.

Erdogan, A. J., Ali, M., Habich, M., Salscheider, S. L., Schu, L., Petrungaro, C., Thomas, L. W., Ashcroft, M., Leichert, L. I., Roma, L. P., and Riemer, J. (2018). The mitochondrial oxidoreductase CHCHD4 is present in a semi-oxidized state in vivo. Redox Biol. 17, 200-206.

Mattie, S., Riemer, J., Wideman, J.G., McBride, H.M. (2018). A new mitofusin topology places the redox-regulated C terminus in the mitochondrial intermembrane space. J Cell Biol. 217, 507-515.

Meyer, A.J., Riemer, J., and Rouhier, N. (2018). Oxidative protein folding: state-of-the-art and current avenues of research in plants. New Phytol. 221, 1230-1246.

Erdogan, A. J. and J. Riemer (2017). Mitochondrial disulfide relay and its substrates: mechanisms in health and disease. Cell Tissue Res. 367, 59-72.

Friederich, M.W., Erdogan, A.J., Coughlin, C.R., Elos, M.T., Jiang, H., O'Rourke, C.P., Lovell, M.A., Wartchow, E., Gowan, K., Chatfield, K.C., Chick, W.S., Spector, E.B., Van Hove, J.L.K., and Riemer, J. (2017). Mutations in the accessory subunit NDUFB10 result in isolated complex I deficiency and illustrate the critical role of intermembrane space import for complex I holoenzyme assembly. Hum. Mol. Genet. 26, 702-716.

Calabrese, G. Morgan, B., and Riemer, J. (2017). Mitochondrial Glutathione: Regulation and Functions. Antioxid. Redox Signaling 27, 1162-1177.

Habich, M. and Riemer, J. (2017). Detection of Cysteine Redox States in Mitochondrial Proteins in Intact Mammalian Cells. In: Mokranjac, D., Perocchi, F. (eds). Mitochondria. Methods in Molecular Biology, Vol 1567. Humana Press, New York, NY.

Döring, K., Ahmed, N., Riemer, T., Suresh, H.G., Vainshtein, Y., Habich, M., Riemer, J., Mayer, M.P., O'Brien, E.P., Kramer, G., and Bukau B. (2017). Profiling Ssb-Nascent Chain Interactions Reveals Principles of Hsp70-Assisted Folding. Cell. 170, 298-311.