Protein Quality Control
Head: Dr. Christian Münch
Mitochondria are essential for most cellular processes and a cell’s very own survival. To remain active and functional, mitochondria need to control the synthesis and folding of their proteins. However, many cellular perturbations, including major diseases like neurodegenerative diseases and cancer, can harm mitochondria’s protein folding homeostasis, with potentially fatal consequences for cells.
|Research in the Münch laboratory focuses on the mitochondrial protein quality control responses in mammalian cells upon mitochondrial protein misfolding, particularly the mitochondrial unfolded protein response (UPRmt). During protein folding stress in mitochondria, UPRmt elicits a transcriptional response to induce genes such as chaperonins to increase the mitochondrial folding capacity. Additionally, as we recently showed, UPRmt also contains a translational response that reduces the folding load of proteins inside mitochondria by reversibly halting mitochondrial translation (Figure). We aim to further understand and define the processes involved in the UPRmt and other mitochondrial stress responses upon protein misfolding and to gain insight into the pathways that protect from mitochondrial and cellular damage. The lab heavily relies on our expertise in quantitative mass spectrometry in combination with cutting-edge cell biological, biochemical, gene editing, and next-generation sequencing approaches as tools to address our biological questions.
We are grateful to the funders of our work: The Emmy Noether Program (DFG), HMWK LOEWE Center for Cell and Gene Therapy, and CRC 1177 on Selective Autophagy (SFB).