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Dnm1 forms spirals that are structurally tailored to fit mitochondria

¹ Department of Molecular and Cellular Biology, Center for Genetics and Development, University of California, Davis, Davis, CA 95616
² Department of Biology and Integrated Imaging Center, Johns Hopkins University, Baltimore, MD 21218
³ Laboratory of Cell Biochemistry and Biology, National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases, National Institutes of Health (NIH), Bethesda, MD 20892

Correspondence to Jodi Nunnari: jmnunnari{at}ucdavis.edu; or Jenny E. Hinshaw: jennyh{at}helix.nih.gov

Abstract

Dynamin-related proteins (DRPs) are large self-assembling GTPases whose common function is to regulate membrane dynamics in a variety of cellular processes. Dnm1, which is a yeast DRP (Drp1/Dlp1 in humans), is required for mitochondrial division, but its mechanism is unknown. We provide evidence that Dnm1 likely functions through self-assembly to drive the membrane constriction event that is associated with mitochondrial division. Two regulatory features of Dnm1 self-assembly were also identified. Dnm1 self-assembly proceeded through a rate-limiting nucleation step, and nucleotide hydrolysis by assembled Dnm1 structures was highly cooperative with respect to GTP. Dnm1 formed extended spirals, which possessed diameters greater than those of dynamin-1 spirals but whose sizes, remarkably, were equal to those of mitochondrial constriction sites in vivo. These data suggest that Dnm1 has evolved to form structures that fit the dimensions of mitochondria.

Abbreviations used in this paper: DRP, dynamin-related protein; GDP, guanosine 5'-diphosphate; GED, GTPase effector domain; GMP-PCP, ß,-methyleneguanosine 5'-triphosphate; PEP, phosphoenolpyruvate.

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