Abstract
Mitochondrial fission is mediated by a dynamin-related GTPase that assembles at constricted sites on the organelle. The mechanism of action of this GTPase in fission is related to that of classical dynamin, which severs the necks of clathrin-coated pits at the plasma membrane. The scale of these membrane remodeling events differs by an order of magnitude, however, and structural studies have revealed variations in the assembly properties of classical and mitochondrial dynamins that accommodate these differences. Despite this progress, structural and mechanistic models have not yet incorporated a growing number of adaptor proteins that are required for the membrane recruitment and function of mitochondrial dynamins. Here, we review the structure and assembly properties of the yeast and mammalian mitochondrial dynamins and discuss what is known about the activities of their adaptor proteins.