Abstract
Dynamin-related protein 1 (Drp1) belongs to a family of large GTPase proteins that regulate membrane dynamics and morphology. Self-assembly of cytosolic Drp1 into larger oligomers on the surface of mitochondria is essential for ensuing membrane fission. Preliminary studies show that in vitro reconstitutions of Drp1 emulate key features of the mitochondrial division machinery and provide a model system for evaluating conformational changes that drive membrane remodeling. To understand Drp1 self-assembly, cryo-electron microscopy (cryo-EM) will be used to determine the 3D structures of both the pre-assembly state and helical oligomers. More specifically, recombinant Drp1 forms stable tetramers in solution that are amenable to EM analysis. In the presence of non-hydrolyzable GTP analogs and/or synthetic liposomes, Drp1 further assembles into helical oligomers with varying diameters, suggesting ligand-induced conformational changes. Cryo-EM studies will determine the 3D structures of reconstituted Drp1 oligomers to reveal key intermolecular interactions and conformational changes that drive Drp1 self-assembly and mediate mitochondrial membrane fission.
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