Dr. Oliver Daumke
Max-Delbrück-Center for Molecular Medicine (MDC)
Max Delbrück House (Flachbau, 31.2), Room: 0225
13125 Berlin, Germany
Phone: +49 30 9406 3425
oliver.daumke [at] mdc-berlin.de
G-proteins in membrane remodelling
Guanine nucleotide binding proteins (G-proteins) are involved in a diverse range of cellular processes including protein synthesis, sensual perception, vesicular transport and signal transduction cascades. Whereas small G-proteins are molecular switches that cycle between an active GTP-bound form and an inactive GDP-bound form, large G-proteins of the dynamin superfamily are mechano-chemical enzymes that use the energy of GTP hydrolysis to actively remodel membranes. Members of both groups bind to membranes, and this interaction is crucial for their function. Our projects aim to elucidate the interaction and reciprocal modulation of membranes and G-proteins using structural, biochemical and cell-biological methods.
Since 2008 | Helmholtz University Junior Group Leader at the Max-Delbrück Centrum for Molecular Medicine, Berlin
2004 - 2007 | Postdoctoral Fellow at the Laboratory of Molecular Biology (Cambridge, UK) with HT McMahon
Currently, my group consists of 1 PostDoc, 5 PhD students and 2 technical assistants and I have no teaching obligations.
2001-2004 | PhD Studies at the Max-Planck Institute in Dortmund with A. Wittinghofer: “Structural and functional analysis of Rap1GAP” (summa cum laude)
2000 Diplomarbeit at the University of Cologne (very good)
1995-2000 | Studies in Biology at the Universities of Freiburg, Sussex (UK) and Cologne
Selbach, M, Paul FE, Brandt S, Guye, P, Daumke, O, Backert, S, Dehio, C, Mann M. (2009) Host cell interactome of tyrosine-phosphorylated bacterial proteins. Cell Host Microbe, 5, 397-403
Daumke, O, Lundmark R, Vallis, Y, Martens, S, Butler, PJ, McMahon HM. (2007) Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling. Nature, 449, 923-927.
Henne, WM, Kent, HM, Ford, MG, Hegde, BG, Daumke, O, Butler, PJ, Mittal, R, Langen, R, Evans, PR, McMahon, HT. (2007) Structure and analysis of FCHo2 F-BAR domain: A dimerizing and membrane recruitment module that effects membrane curvature. Structure, 15, 839-852.
Kupzig, S, Deaconescu, D, Bouyoucef, D, Walker SA, Liu Q, Polte, CL, Daumke, O, Ishizaki, T, Lockyer, PJ, Wittinghofer, A, Cullen PJ. (2006) GAP1 family members constitute bifunctional RAS and RAP GTPase-activating proteins. J Biol Chem, 281, 9891-9900.
Daumke, O, Weyand , M, Chakrabarti PP, Vetter I, Wittinghofer A. (2004). The GTPase activating protein Rap1GAP uses a catalytic asparagine. Nature, 429, 197-201