Roland Lill
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Prof. Dr. Roland Lill
Institut für Zytobiologie
Philipps-Universität Marburg
Robert-Koch-Str. 6
35037 Marburg - Germany
Phone: +49-6421-286 6449
+49-6421-286 6483 (Sekr.)
Fax: +49-6421-286 6414
E-mail: lill@staff.uni-marburg.de
Research group members
Group leader: Prof. Dr. Roland Lill
Secretary: Gisela Lesch
Senior research fellows: PD Dr. Ulrich Mühlenhoff, PD Dr. Antonio Pierik
Postdoctoral fellows: Dr. Oliver Stehling, Dr. Alex Sheftel, Dr. Judita Mascarenhas, Dr. Sabine Molik, Dr. Daili J.A. Netz, Dr. Torsten Heidenreich
PhD/Diploma/Bachelor students: Holger Webert, Bastian Hoffmann, Marta Uzarska, Sven Freibert
Technical assistants: Nadine Richter, Ralf Rösser, Brigitte Niggemeyer, Martin Stümpfig, Gabriele Köpf
Prof. Dr. Roland Lill
Curriculum Vitae
Roland Lill (born 1955)
Studies in Chemistry, Universities of Ulm and München, 1975-80
Diplom (Biochemistry), University of München, 1980
Dr.rer.nat. (Biochemistry), University of München, 1986
Postdoc as a DFG Fellow, University of California at Los Angeles, 1987-89
Research Associate, Institute for Physiological Chemistry, University of München, 1990-96
Leader of a project in the Collaborative Research Center SFB 184, University of München 1993-96
Professor for Cell Biology, Institute for Cell Biology, University of Marburg, since 1996
Director of the Institute for Cell Biology, University of Marburg, since 2002
Coordinator of the Collaborative Research Center SFB 593, University of Marburg, since 2003
Max Planck Fellow at the MPI Marburg, since 2008
Research area: Biogenesis of iron-sulfur proteins in eukaryotes and the link to cellular iron homeostasis.
Iron-sulfur (Fe/S) clusters are ubiquitous and versatile protein cofactors used for catalysis, electron transfer and sensing. In a living cell these simple inorganic cofactors are synthesized and inserted into apoproteins by a surprisingly complex proteinaceous machinery involving the ISC assembly and export machineries of mitochondria, and the CIA machinery of the cytosol. Our group is interested in understanding the molecular mechanisms of Fe/S protein maturation. We use yeast and human cell culture as model systems. Since the efficiency of Fe/S protein maturation is intimately linked to cellular iron uptake and homeostasis, we are trying to understand both the mechanisms of iron uptake regulation and the molecular basis that connects both processes.
Selected publications
Sheftel, A.D., Stehling, O., Pierik, A.J., Elsässer, H.P., Mühlenhoff, U., Webert, H., Hobler, A., Hannemann, F., Bernhardt, R., & Lill, R. (2010). Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct functions in steroidogenesis, heme and Fe/S cluster biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 107, 11775-11780.
Mühlenhoff, U., Molik, S., Godoy, J.R., Uzarska, M.A., Richter, N., Seubert, A., Zhang, Y., Stubbe, J., Pierrel, F., Herrero, E., Lillig, C.H. & Lill, R. (2010). Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster. Cell Metab. 12 , 373-385.
Netz, D.J.A., Stümpfig, M., Doré, C., Mühlenhoff, U., Pierik, A.J. & Lill, R. (2010). Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis. Nature Chem. Biol. 6, 758-765.
Commentary by DosSantos and Dean (2010) Nature Chem. Biol. 6, 700-701.
Lill, R. (2009). Function and biogenesis of iron-sulphur proteins. Nature 460, 831-838.
Lill, R. & Mühlenhoff, U. (2006). Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms. Annu. Rev. Cell Dev. Biol. 22, 457-486.
Goldberg, A.V.*, Molik, S.*, Tsaousis, A.D., Neumann, K., Kuhnke, G., Delbac, F., Vivares, C.P., Hirt, R.P., Lill, R.# & Embley, M.# (2008). Localization and functionality of microsporidian iron-sulphur cluster assembly proteins. Nature 452, 624-628. Joint first* and joint corresponding# authors.
Netz, D.J.A., Pierik, A.J., Stümpfig, M., Mühlenhoff, U., & Lill, R. (2007). The Cfd1/Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol. Nature Chem. Biol. 3, 278-286.