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B02 - Hydrogen peroxide signalling in mitochondrial communication

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.


Abstract
The release of hydrogen peroxide (H2O2) from mitochondria has been implicated in regulating processes inside and outside of the organelle. H2O2 is an elegant choice as mitochondrial signalling molecule because its production integrates inputs from mitochondrial activity, the availability of redox enzymes and cellular metabolism. At present it is unclear how much H2O2 is produced by mitochondria in intact cells and what protein targets of H2O2 signalling are. We will investigate the spatiotemporal pattern of mitochondrial H2O2 release using novel genetically-encoded fluorescent sensors. We will identify targets of mitochondria-derived H2O2 using quantitative redox proteomics. We will thereby 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.


Latest publications
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.

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.

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., and Riemer J. (2016). 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. pii: ddw431. doi: 10.1093/hmg/ddw431. [Epub ahead of print]