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The dynamin family of GTPases is essential for receptor-mediated endocytosis and synaptic vesicle recycling, and it has recently been shown to play a role in vesicle formation from the trans-Golgi network (1). Dynamin-1 is a GTP-, microtubule-, and phospholipid-binding protein that is expressed primarily in brain and almost exclusively expressed in the central nervous system (2). Dynamin-1 is believed to assemble around the necks of clathrin-coated pits and assist in pinching vesicles from the plasma membrane. This role would make dynamin unique among GTPases in its ability to act as a mechanochemical enzyme (1). Dynamin-1 function is apparently essential for scission of newly formed vesicles from the plasma membrane; it has been proposed that dynamin is a regulator of downstream effectors of scission, rather than being directly responsible for it (3).
