Dynamic Organization of Cellular Protein Machineries: From Biogenesis and Modular Assembly to Function Research Program
Dynamic Organization of Cellular Protein Machineries: From Biogenesis and Modular Assembly to Function Projects

The Goal of the SFB 1381

The SFB 1381 investigates how different proteins are dynamically assembled into complex multimers, the so-called protein machineries, which play a central role e.g. in the energy metabolism of the cell, the replication, repair, and transcription of DNA, the folding and degradation of proteins, as well as the intra- and intercellular communication and transport processes. The focus of the SFB 1381 lies on the organization of these protein machineries in modular units, the regulation of their assembly and disassembly, and the impact of these processes on cellular functions.

The aim of the SFB 1381 is to define and understand the dynamic processes of the assembly and organization of cellular protein machineries, and to gain insight into the fundamental processes in a living cell.

Research Program


Imagefilm of SFB 1381. Video Jürgen Gocke. Also available on Youtube


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Mondol, T., Silbermann, L.M., Schimpf, J., Vollmar, L., Hermann, B., Tych, K.K., Hugel, T. (2023) Aha1 regulates Hsp90’s conformation and function in a stoichiometry-dependent way. Biophys J. 122(17), 3458-3468
Lan, C., Kim, J., Ulferts, S., Aprile-Garcia, F., Weyrauch, S., Anandamurugan, A., Grosse, R., Sawarkar, R., Reinhardt, A., Hugel, T. (2023) Quantitative real-time in-cell imaging reveals heterogeneous clusters of proteins prior to condensation. Nat Commun. 14(1), 4831

Schulte, U., den Brave, F., Haupt, A., Gupta, A., Song, J., Müller, C. S., Engelke, J., Mishra, S., Mårtensson, C., Ellenrieder, L., Priesnitz, C., Straub, S. P., Doan, K. N., Kulawiak, B., Bildl, W., Rampelt, H., Wiedemann, N., Pfanner, N., Fakler, B., and Becker, T. (2023) Mitochondrial complexome reveals quality-control pathways of protein import. Nature, online ahead of print

Vögtle, F.N., Koch, H.G., and  Meisinger, C. (2022) A common evolutionary origin reveals fundamental principles of protein insertases. PLoS Biol 20(3), e3001558

Morgenstern, M., Peikert, C.D., Lübbert, P., Suppanz, I., Klemm, C., Alka, O., Steiert, C., Naumenko, N., Schendzielorz, A., Melchionda, L., Mühlhäuser, W.W.D., Knapp, B., Busch, J.D., Stiller, S.B., Dannenmaier, S., Lindau, C., Licheva, M., Eickhorst, C., Galbusera, R., Zerbes, R.M., Ryan, M.T., Kraft, C., Kozjak-Pavlovic, V., Drepper, F., Dennerlein, S., Oeljeklaus, S., Pfanner, N., Wiedemann, N., and Warscheid, B. (2021) Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context. Cell. Metab. 33(12), 2464-2483, e18

Yousefi, O.S., Ruggieri, M., Idstein, V., von Prillwitz, K.U., Herr, L.A., Chalupsky, J., Köhn, M., Weber, W., Timmer, J., and Schamel, W.W.A. (2021) Cross-TCR Antagonism Revealed by Optogenetically Tuning the Half-Life of the TCR Ligand Binding. Int. J. Mol. Sci. 22, 4920

Agne, M., Estelmann, S., Seelmann, C. S., Kung, J., Wilkens, D., Koch, H.G., van der Does, C., Albers, S. V., von Ballmoos, C., Simon, J., and Boll, M. (2021) The missing enzymatic link in syntrophic methane formation from fatty acid. Proc. Natl. Acad. Sci. U S A 118(40), e2111682118

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