Research in the Riemer lab
Our laboratory works on the redox control of cellular processes, and on mitochondria and their integration into cellular signalling and biogenesis networks.
Redox reactions are at the centre of most cellular processes: they are at the mechanistic heart of metabolic pathways, they contribute to proteostasis e.g. by the introduction and removal of disulphide bonds, and they drive the production of reactive oxygen species (ROS), which - with their Janus-faced character of being on the one hand toxic and on the other essential for signalling - impact heavily on cellular physiology. A number of diseases have been directly linked with dysregulated redox homeostasis, including cancer, neurological disorders, cardiovascular diseases, obesity and metabolic diseases, as well as aging. We aim to understand in molecular detail how redox homeostasis is maintained in the different compartments of a cell, how mitochondria as major ROS generators are integrated into cellular signalling networks, how redox processes drive mitochondrial biogenesis, and how organellar proteome plasticity is driven by metabolic and redox changes e.g. during cell differentiation.
We employ a combination of biochemical and cell biological methods ranging from in vitro reconstitution experiments of whole enzymatic cascades, via different proteomics approaches to tackle specific redox changes and complex assembly processes, genetic screens using CRISPR-Cas technology to the application of genetically encoded sensors and engineering tools. As model systems, we rely on mammalian cell culture, on mice and baker’s yeast.
Redox Signalling and Mitochondria as Signalling Organelles
Redox Processes in Mitochondrial Biogenesis and Proteostasis
Metabolic and Redox Regulation of Proteome Plasticity
Please have a look at our recent reviews
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Jacobs LJHC, Riemer J. (2023) Maintenance of small molecule redox homeostasis in mitochondria. FEBS Lett. 597(2):205-223
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Habich M, Salscheider SL, Riemer J. (2019) Cysteine residues in mitochondrial intermembrane space proteins: more than just import. Br J Pharmacol. 176(4):514-531