Nora Voegtle Welcome to the future Voegtle lab!
Mitochondria are essential organelles well known for their role in ATP synthesis, multiple metabolic pathways or programmed cell death. They form a dynamic elongated network and are integrated into the cellular signalling network. To fulfill their various functions mitochondria have to build and maintain a complex proteome of more than 1000 different proteins. The vast majority of these mitochondrial proteins is imported post-translationally into the organelle and requires proteolytic processing to mature into functional and stable proteins. We are interested in the proteases that perform this processing and subsequent quality control of the incoming precursors.
Recent Research Highlights
Current Research
Mitochondria are essential organelles well known for their role in ATP synthesis, multiple metabolic pathways or programmed cell death. They form a dynamic elongated network and are integrated into the cellular signalling network. To fulfill their various functions mitochondria have to build and maintain a complex proteome of more than 1000 different proteins. The vast majority of these mitochondrial proteins is imported post-translationally into the organelle and requires proteolytic processing to mature into functional and stable proteins. We are interested in the proteases that perform this processing and subsequent quality control of the incoming precursors.
5 Selected publications
Original Research Papers
Kücükköse, C., Taskin, A.A., Marada, A., Brummer, T., Dennerlein, S., and Vögtle, F.N. (2021). Functional coupling of presequence processing and degradation in human mitochondria. FEBS J., 288, 600-613.
Poveda-Huertes, D., Matic, S., Marada, A., Habernig, L., Licheva, M., Myketin, L., Gilsbach, R., Tosal-Castano, S., Papinski, D., Mulica, P., Kretz, O., Kücükköse, C., Taskin, A.A., Hein, L., Kraft. C., Büttner, S., Meisinger, C., and Vögtle, F.N. (2020). An early mtUPR: Redistribution of the nuclear transcription factor Rox1 into mitochondria protects against intramitochondrial proteotoxic aggregates. Mol. Cell 77, 180-188.
Vögtle, F.N.#,*, Brändl, B.*, Larson, A.*, Pendziwiat, M.*, Friederich, M.W.*, White, S.M., Basinger, A., Kücükköse, C., Muhle, H., Jähn, J.A., Keminer, O., Helbig, K.L., Delto, C.F., Myketin, L., Mossmann, D., Burger, N., Miyake, N., Burnett, A., van Baalen, A., Lovell, M.A., Matsumoto, N., Walsh, M., Yu, H.C., Shinde, D.N., Stephani, U., Van Hove, J.L.K., Müller, F.J., Helbig, I.# (2018). Mutations in PMPCB Encoding the Catalytic Subunit of the Mitochondrial Presequence Protease Cause Neurodegeneration in Early Childhood. Am. J. Hum. Genet. 102, 557-573.
Vögtle, F.N.*, Burkhart, J.M.*, Gonczarowska-Jorge, H., Kücükköse, C., Taskin, A.A., Kopczynski, D., Ahrends, R., Mossmann, D., Sickmann, A., Zahedi, R.P., and Meisinger, C. (2017). Landscape of submitochondrial protein distribution. Nat. Commun. 8, 290.
Taskin, A.A., Kücükköse, C., Burger, N., Mossmann, D., Meisinger, C., and Vögtle, F.N. (2017). The novel mitochondrial matrix protease Ste23 is required for efficient presequence degradation and processing. Mol. Biol. Cell 28, 997-1002.
* equal contribution
# corresponding author