Prof. Nora Vögtle, Ruprecht-Karls-Universität Heidelberg

Mitochondria contain more than 1000 different proteins, the vast majority of which are imported as precursors from the cytosol. Most precursors use N-terminal presequences as targeting signals that are proteolytically removed upon import into the mitochondrial matrix. Processing of the precursors and subsequent turnover of the targeting peptides is carried out by specific presequence proteases and peptidases. Mutations in these enzymes can cause severe human diseases, such as neurodegeneration or cardiomyopathies. We are investigating the physiological functions and interactions of this protease network and how it shapes and maintains the mitochondrial proteome. In particular, we focus on the pathophysiological consequences of disease mutations and how the cell deals with dysfunction in the cellular powerhouse.