Dynamin

Dynamin is a large GTPase enzyme critical for the scission of budding vesicles from cellular membranes, particularly in clathrin-mediated endocytosis and synaptic vesicle recycling[1][5]. It is part of the dynamin superfamily, alongside proteins involved in membrane fusion and fission events in organelles such as mitochondria and peroxisomes[1][2]. Mammalian cells express multiple isoforms: Dynamin-1 (neuronal), Dynamin-2 (ubiquitous), and Dynamin-3 (testis/brain-specific), each adapted for specialized roles in vesicle trafficking[1]. Dynamin assembles into spirals around vesicle necks, and upon GTP hydrolysis, it constricts and induces membrane fission[1][3]. It plays a key role in coupling signal transduction (via receptor-mediated endocytosis), cellular trafficking, and cytoskeletal remodeling[4]. Pharmacological inhibitors such as Dynasore have enabled detailed dissection of its function but raise safety concerns due to the broad physiological roles of dynamin[1]. Dynamin has emerging significance as a therapeutic target in models of neurodegeneration, cancer, and infection, where abnormal trafficking or altered endocytosis is involved[1][5].

Other names

DNM1 (gene name for Dynamin-1)DNM2 (Dynamin-2)DNM3 (Dynamin-3)Dynamin superfamily proteinMechano-GTPase

Inhibition of GTPase activity Disruption of dynamin-mediated membrane scission