Structure and Membrane Interaction of G-Proteins


Head of the Group

Prof. Dr. Oliver Daumke

31.2: Max Delbrück House (Flachbau)

Room 0225

Tel. 9406-3425



GTPases of the dynamin and septin superfamilies assemble at the surfaces of cellular membranes into highly organized scaffolds which can remodel membranes or orchestrate the recruitment of interaction partner in a temporally and spatially controlled manner. Together with partner proteins, these scaffolds constitute cellular modules which perform essential functions, such as membrane scission and fusion or the control of antiviral activity. Dysfunction of these GTPases is implicated in many diseases, such as cancer, viral infections or neurodegenerative diseases.

Dynamin superfamily GTPases are multi-domain proteins with a common domain architecture. They are comprised of an amino-terminal GTPase domain, followed by one or more helical domains. Additional domains, such as the pleckstrin homology (PH) domain in dynamin, mediate membrane binding or regulate the assembly.

A common principle of these GTPases is the GTP-dependent assembly of their GTPase domains. Often, this assembly results in activation of the GTPase activity. The ensuing conformational changes are relayed from the GTPase domain to the helical domains leading to conformational changes in the oligomer and remodeling of the underlying membrane. Therefore, these proteins are considered as mechano-chemical enzymes. In the GDP-bound form, the GTPase domains dissociate.

My group is interested to understand the molecular mechanism of assembly and the structural basis of the mechano-chemical function in these GTPases. To this end, we combine structural studies with biochemical and cell-based approaches. We also collaborate with several groups in and outside of Berlin to elucidate together structure and function of other membrane-associated proteins.