zum Inhalt springen


Mitochondria are highly dynamic organelles with critical importance for the cell. To fulfill their various functions and to adjust to different cellular demands, their proteome needs to be highly plastic with respect to its quantity (amounts, activity) and quality (different proteins). This requires a dynamic regulation of mitochondrial biogenesis, protein import, and protein homeostasis on different levels. In this project, we will investigate a novel mechanism that controls dual localization of mitochondrial proteins. Here, cytosolic processing of protein N-termini renders specific precursor proteins susceptible to proteasomal degradation, ensuring that they are only present in mitochondria. On the other hand, preventing this processing sustains a functional non-mitochondrial protein pool.

Selected Publications

  • Habich M, Salscheider SL, Murschall LM, Hoehne MN, Fischer M, Schorn F, Petrungaro C, Ali M, Erdogan AJ, Abou-Eid S, Kashkar H, Dengjel J, 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 Reports 15;26(3):759-774

  • Friederich MW, Erdogan AJ, Coughlin CR, Elosa M, Jiang H, O’Rourke C, Lovell MA, Wartchow E, Gowan K, Chatfield KC, Chick WS, Spector E, Van Hove JLK, 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(4):702-716

  • Erdogan, A.J. and J. Riemer (2017) Mitochondrial disulfide relay and its substrates: mechanisms in health and disease. Cell Tissue Res, 367(1): p. 59-72.