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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Selected Publications

Njenga, R. K., Boele, J., Drepper, F., Sinha, K., Marouda, E., Huesgen, P. F., Blaby-Haas, C. and Koch, H. G. (2024) Ribosome-inactivation by a class of widely distributed C-tail anchored membrane proteins. Structure Online ahead of print

Marada, A., Walter, C., Suhm, T., Shankar, S., Nandy, A., Brummer, T., Dhaouadi, I., Vogtle, F. N. and Meisinger, C. (2024) DYRK1A signalling synchronizes the mitochondrial import pathways for metabolic rewiring. Nat Commun 15(1), 5265

Eickhorst, C., Babic, R., Rush-Kittle, J., Lucya, L., Lami Imam, F., Sanchez-Martin, P., Hollenstein, D. M., Michaelis, J., Munch, C., Meisinger, C., Slade, D., Gamez-Diaz, L. and Kraft, C. (2024) FIP200 phosphorylation regulates late steps in mitophagy. J Mol Biol 168631

Busto, J. V., Ganesan, I., Mathar, H., Steiert, C., Schneider, E. F., Straub, S. P., Ellenrieder, L., Song, J., Stiller, S. B., Lubbert, P., Chatterjee, R., Elsaesser, J., Melchionda, L., Schug, C., den Brave, F., Schulte, U., Klecker, T., Kraft, C., Fakler, B., Becker, T. and Wiedemann, N. (2024) Role of the small protein Mco6 in the mitochondrial sorting and assembly machinery. Cell Rep 43(3), 113805

Moretti-Horten, D. N., Peselj, C., Taskin, A. A., Myketin, L., Schulte, U., Einsle, O., Drepper, F., Luzarowski, M. and Vogtle, F. N. (2024) Synchronized assembly of the oxidative phosphorylation system controls mitochondrial respiration in yeast. Dev Cell 9(8), 1043-1057 e1048

Vollmar, L., Schimpf, J., Hermann, B. and Hugel, T. (2024) Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90. Nat. Commun. 15, 569

Velasco Cárdenas, R.MH., Brandl, S.M., Meléndez, A.V., Schlaak, A.E., Buschky, A.,  Peters, T., Beier, F., Serrels, B., Taromi, S., Raute, K., Hauri, S., Gstaiger, M., Lassmann, S., Huppa, J.B., Boerries, M., Andrieux, G., Bengsch, B., Schamel, W.W. and Minguet, S. (2023) Harnessing CD3 diversity to optimize CAR T cells. Nat. Immunol. 24, 2135–2149

Guhathakurta, S., Erdogdu, N. U., Hoffmann, J. J., Grzadzielewska, I., Schendzielorz, A., Seyfferth, J., Martensson, C. U., Corrado, M., Karoutas, A., Warscheid, B., Pfanner, N., Becker, T. and Akhtar, A. (2023) COX17 acetylation via MOF-KANSL complex promotes mitochondrial integrity and function. Nat Metab 5(11), 1931-1952

Lan, C., Kim, J., Ulferts, S., Aprile-Garcia, F., Weyrauch, S., Anandamurugan, A., Grosse, R., Sawarkar, R., Reinhardt, A. and Hugel, T. (2023) Quantitative real-time in-cell imaging reveals heterogeneous clusters of proteins prior to condensation. Nat. Commun. 14(1), 4831

Fielden, L.F., Busch, J.D., Merkt, S.G., Ganesan, I., Steiert, C., Hasselblatt, H.B., Busto, J.V., Wirth, C., Zufall, N., Jungbluth, S., Noll, K., Dung, J.M., Butenko, L., von der Malsburg, K., Koch, H.G., Hunte, C., van der Laan, M., and Wiedemann, N. (2023) Central role of Tim17 in mitochondrial presequence protein translocation. Nature 621, 627–634

Xu, F., Li, R., von Gromoff, E. D., Drepper, F., Knapp, B., Warscheid, B., Baumeister, R. and Qi, W. (2023) Reprogramming of the transcriptome after heat stress mediates heat hormesis in Caenorhabditis elegans. Nat Commun 14(1), 4176

Becker, F., Fuchs, S., Refisch, L., Drepper, F., Bildl, W., Schulte, U., Liang, S., Heinicke, J. I., Hansen, S. C., Kreutz, C., Warscheid, B., Fakler, B., Mymrikov, E. V. and Hunte, C. (2023) Conformational regulation and target-myristoyl switch of calcineurin B homologous protein 3. Elife 12

Sarmah, P., Shang, W., Origi, A., Licheva, M., Kraft, C., Ulbrich, M., Lichtenberg, E., Wilde, A.  and Koch, H.G. (2023) mRNA targeting eliminates the need for the signal recognition particle during membrane protein insertion in bacteria. Cell Reports 42(3), 112140

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 614, 153–159

Gaines, M. C., Isupov, M. N., Sivabalasarma, S., Haque, R. U., McLaren, M., Mollat, C. L., Tripp, P., Neuhaus, A., Gold, V. A. M., Albers, S. V., and Daum, B. (2022) Electron cryo-microscopy reveals the structure of the archaeal thread filament. Nat Commun. 13(1), 7411

van Wolferen, M., Pulschen, A. A., Baum, B., Gribaldo, S., and Albers, S. V. (2022) The cell biology of archaea. Nat Microbiol. 7(11), 1744-1755

Diessl, J., Berndtsson, J., Broeskamp, F., Habernig, L., Kohler, V., Vazquez-Calvo, C., Nandy, A., Peselj, C., Drobysheva, S., Pelosi, L., Vögtle, F. N., Pierrel, F., Ott, M., and Büttner, S. (2022) Manganese-driven CoQ deficiency. Nat Commun. 13(1), 6061

Götz, M., Barth, A., Bohr, S., Börner, R., Chen. J., Cordes, T., Erie, D., Gebhardt, C., Hadzic, M., Hamilton, G., Hatzakis, N., Hugel, T., Kisley, L., Lamb, D., de Lannoy, C., Mahn, C., Dunukara., D., de Ridder, D., Sanabria, H., Schimpf, J., Seidel, C., Sigel, R., Sletfjerding, M., Thomsen, J., Vollmar, L., Wanninger, S., Weninger, K., Xu, P., and Schmid, S. (2022) A blind benchmark of analysis tools to infer kinetic rate constants from single-molecule FRET trajectories. Nat. Commun. 13, 5402

Müller, C., Zhang, L., Zipfel, S., Topitsch, A., Lutz, M., Eckert, J., Prasser, B., Chami, M., Lü, W., Du, J., and Einsle, O. (2022) Molecular interplay of an assembly machinery for nitrous oxide reductase. Nature 608, 626-631

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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