Proteins of the dynamin superfamily are mechanochemical GTPases, which mediate
nucleotide-dependent membrane remodeling events. The founding member dynamin is
recruited to the neck of clathrin-coated endocytic vesicles where it oligomerizes into helical
filaments. Nucleotide-hydrolysis-induced conformational changes in the oligomer catalyze
scission of the vesicle neck. Here, we review recent insights into structure, function, and
oligomerization of dynamin superfamily proteins and their roles in human diseases. We …