Brief Communication abstract
Nature Cell Biology 3, 922 - 926 (2001)
Published online: 13 September 2001 | doi:10.1038/ncb1001-922
Three-dimensional reconstruction of dynamin in the constricted state
Peijun Zhang1 & Jenny E. Hinshaw1
Members of the dynamin family of GTPases have unique structural properties that might reveal a general mechanochemical basis for membrane constriction. Receptor-mediated endocytosis, caveolae internalization and certain trafficking events in the Golgi all require dynamin for vesiculation1. The dynamin-related protein Drp1 (Dlp1) has been implicated in mitochondria fission2 and a plant dynamin-like protein phragmoplastin is involved in the vesicular events leading to cell wall formation3. A common theme among these proteins is their ability to self-assemble into spirals and their localization to areas of membrane fission. Here we present the first three-dimensional structure of dynamin at a resolution of 
20 Å, determined from cryo-electron micrographs of tubular crystals in the constricted state. The map reveals a T-shaped dimer consisting of three prominent densities: leg, stalk and head. The structure suggests that the dense stalk and head regions rearrange when GTP is added, a rearrangement that generates a force on the underlying lipid bilayer and thereby leads to membrane constriction. These results indicate that dynamin is a force-generating 'contrictase'.
- Laboratory of Cell Biochemistry and Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Building 8, Room 419, MSC 0851, 8 Center Drive, National Institutes of Health, Bethesda, Maryland 20892, USA
Correspondence to: Jenny E. Hinshaw1 e-mail: jennyh@helix.nih.gov
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