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Mitochondria are central metabolic hubs that dynamically adapt to changing metabolic cues and environmental challenges. Mitochondrial reprogramming is accompanied by alterations in the mitochondrial proteome, which can be the result of changes in the expression and stability of mitochondrial proteins or in their cellular localization. Regulated cleavage by the mitochondrial protease PARL is a novel mechanism driving dual protein localization and thereby ensuring coordination of mitochondrial function with cellular activities. In this project, we will explore the regulation of the cellular localization of mitochondrial proteins by PARL and its influence on cellular lipid transfer.

Selected Publications

  • Saita, S., T. Tatsuta, P.A. Lampe, T. Konig, Y. Ohba, and T. Langer (2018), PARL partitions the lipid transfer protein STARD7 between the cytosol and mitochondria. EMBO J. 37(4).

  • Saita, S., H. Nolte, K.U. Fiedler, H. Kashkar, A.S. Venne, R.P. Zahedi, M. Kruger, and T. Langer (2017), PARL mediates Smac proteolytic maturation in mitochondria to promote apoptosis. Nat Cell Biol. 19(4): p. 318-328.

  • Wai, T., Saita, S., Nolte, H., Müller, S., König, T., Richter-Dennerlein, R., Sprenger, H.-G., Madrenas, J., Mühlmeister, M., Brandt, U., Krüger, M., and Langer, T. (2016) The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i-AAA protease YME1L. EMBO Rep. 17, 1844-1856.