Structural and functional analysis of the dynamin module (C07)

• Subject Area: Biochemistry
• Term: from 2008 to 2018
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 25065445

Dynamin oligomerizes around the neck of clathrin-coated vesicles and induces membrane scission in response to nucleotide hydrolysis. Based on the crystal structure of dynamin, we proposed a reversible and flexible assembly of the dynamin helix. In the coming period, we will investigate the molecular mechanisms of the nucleotide-driven mechano-chemical function of the dynamin, the principles of membrane recruitment of dynamin by the BAR-domain containing protein SNX9, and the structural changes in dynamin accompanying membrane recruitment and oligomerization (together with B07, C08, D07).

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 740: From Molecules to Modules: Organisation and Dynamics of Functional Units in Cells
• Applicant Institution: shared FU Berlin and HU Berlin through:; Charité - Universitätsmedizin Berlin
• Co-Applicant Institution: Freie Universität Berlin; Max-Delbrück-Centrum für Molekulare Medizin (MDC)
• Project Head: Professor Dr. Oliver Daumke