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 B7, C8, D7).