Max Delbrück Center for Molecular Medicine
Structure, function and mechanism of dynamin and septin GTPases.
GTPases of the dynamin and septin superfamilies are molecular machines that assemble at the surface of cellular membranes. Some of these proteins act as dynamic scaffolds that remodel the underlying membrane in a GTPase-dependent fashion; others orchestrate the recruitment of interaction partner in a temporally and spatially defined manner. We are interested to understand principles of assembly, function and regulation of these GTPases. To this end, structural studies are combined with biochemical and cell-based approaches.
Reubold TF, Faelber K., Plattner N, Posor Y, Ketel K, Curth U, Schlegel J, Anand R, Manstein DJ, Noé F, Haucke V, Daumke O, Eschenburg S; Crystal structure of the dynamin tetramer. Nature 525, 404-8 (2015). PubMed
Olal D, Dick A, Woods VL, Liu T, Li S, Devignot S, Weber F, Saphire EO, Daumke O; Structural insights into RNA encapsidation and helical assembly of the Toscana virus nucleoprotein. Nucleic Acids Research 42 (9): 6025-6037 (2014-05-31) PubMed
Shah C, Hegde BG, Moren B, Behrmann E, Mielke T, Moenke G, Spahn CM, Lundmark R, Daumke O, Langen R; Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2. Structure 22 (3): 409-420 (2014-03-04) PubMed
Daumke O, Roux A, Haucke V; BAR domain scaffolds in dynamin-mediated membrane fission. Cell 156 (5): 882-892 (2014-02-27) PubMed