Mitarbeiter im Fachbereich Biologie
| Bähler, Martin, Prof. Dr. rer. nat. |  |
| Westfälische Wilhelms-Universität Münster Institut für Molekulare Zellbiologie Schlossplatz 5 D-48149 Münster Tel: + 49 - 251 - 83 2 3841 Fax: + 49 - 251 83 2 4723 E-mail: baehler  net: www.uni-muenster.de/Biologie.AllgmZoo/ | |
| wissenschaftlicher Werdegang | |
| - Studium der Biologie, ETH Zürich - Promotion zum Dr. rer.nat., ETH Zürich - Postoctoral Fellow, The Rockefeller University, New York, USA - Assistant Professor, The Rockefeller University, New York, USA - Leiter einer selbständigen Nachwuchsgruppe, Friedrich Miescher Laboratorium in der Max-Planck Gesellschaft, Tübingen - Habilitation, Eberhard-Karls-Universität Tübingen - Oberassistent, Adolf-Butenandt Institut, LMU München - Professor für Zoologie, Institut für Allgemeine Zoologie und Genetik, WWU Münster | |
| Lehrschwerpunkte | |
| - Zellbiologie - Biochemie - Molekularbiologie | |
| ausgewählte Projekte | |
| Functions of myosin molecules (DFG: SFB 629; GRK1050; Ba 1354/6-1) Myosins are a large family of structurally diverse molecular motors that convert chemical energy derived from ATP-hydrolysis into mechanical force along actin filaments. They are involved in many different cellular processes that are dependent on directed forces like changes in cell morphology, cell migration, cell adhesion, cytokinesis and organelle transport and dynamics. The myosins exhibit different motor properties that are optimally adapted to their respective cellular functions. Furthermore, they have aquired multiple additional functional domains that serve as cargo, cargo receptors or regulatory elements. We are trying to understand how selected myosins function as single molecules, in the cellular context and in the organism. The methodological approaches include a broad set of methods from cell biology, molecular biology, biochemistry, biophysics and mouse technology. Dynamic organization and functions of the actin cytoskeleton (Funding DFG: SPP 1150) A dynamic cytoskeleton allows cells to change their morphology and intracellular organization. These changes in cytoskeletal organization are highly coordinate and complex processes that play important roles in e.g. development, wound healing, immune defense, hearing and cancer. The actin cytoskeleton consists of functionally different subsets of actin filament arrays that coexist in cells. They are populating different or overlapping regions of the cell. Their dynamics and distribution within cells are controlled by a large set of actin-binding proteins. We are studying the functions of particular actin-binding proteins that control the dynamics and organization of actin filament arrays involved in cell migration and macropinocytosis. Macropinocytosis refers to the formation of large endocytic vesicles (macropinosomes), generated by actin-driven circular ruffles of the plasma membrane. Macropinocytosis has an important function in the adaptive immune response, as dendritic cells which present processed antigens to T-cells, take up antigens by macropinocytosis. | |
| ausgewählte Publikationen | |
| Bähler, M., Moser, H., Eppenberger, H.M. and Wallimann, T. (1985) Heart C-protein is transiently expressed during skeletal muscle development in the embryo, but persists in cultured myogenic cells. Devel. Biol. 112: 345-352. Bähler, M. and Greengard, P. (1987) Synapsin I bundles F-actin in a phosphorylation-dependent manner. Nature 326: 704-707. Reinhard, J., Scheel, A.A., Diekmann, D., Hall, A., Ruppert, C. and Bähler, M. (1995) A novel type of myosin implicated in signalling by rho family GTPases. EMBO J. 14: 697-704. Stöffler, H.-E., Ruppert, C., Reinhard, J., and Bähler, M. (1995) A novel mammalian myosin I from rat with an SH3 domain localizes to Con A inducible, F-actin-rich structures at cell-cell contacts. J. Cell Biol. 129: 819-830. Müller, R.T., Honnert, U., Reinhard, J. and Bähler, M. (1997) The myosin myr 5 acts as a RhoGAP in vivo. Essential role of arginine 1695. Mol. Biol. Cell 8: 2039-2053. Stöffler, H.-E., and Bähler, M. (1998)The ATPase activity of purified myr 3, a rat myosin I, is allosterically inhibited by its own tail domain and by Ca2+-binding to its light chain calmodulin. J. Biol. Chem. 273: 14605-14611. Graf, B., Bähler, M., Hilpelä, P., Böwe, C., and Adam, T. (2000) Functional role for the class IX myosin myr5 in epithelial cell infection by Shigella flexneri. Cell. Microbiol. 2: 601-616. Köhler, D., Ruff, C., Meyhöfer, E., and Bähler, M. (2003) Different degrees of lever arm rotation control myosin step size. J. Cell Biol. 161: 237-241. Hilpelä, P., Oberbanscheidt, P., Hahne, P., Hund, M., Kalhammer, G., Small, J.V., and Bähler, M. (2003) SWAP-70 identifies a transitional subset of actin filaments in motile cells. Mol. Biol. Cell 14:3242-3253. Köhler, D., Struchholz, S., and Bähler, M. (2005) The two IQ-motifs and Ca2+/calmodulin regulate the rat myosin 1d ATPase activity. FEBS J. 272: 2189-2197. | |
| ausgewählte Kooperationen | |
| - hochauflösende Elektronenmikroskopie - Einzelmolekülmechanik - Enzymkinetik - Maustechnologie - Antigen präsentierende Zellen - Massenspektroskopie - Kontrolle zellulärer Vorgänge durch Pathogene | |
