Nature Structural & Molecular Biologyv11, 574 - 575 (2004)
Published online: 9 May 2004; | doi:10.1038/nsmb762
The stalk region of dynamin drives the constriction of dynamin tubes
Yen-Ju Chen1, Peijun Zhang2, Edward H Egelman1
& Jenny E Hinshaw2
1
Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia, USA.
2
Laboratory of Cell Biochemistry and Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.
The GTPase dynamin is essential for numerous vesiculation events including clathrin-mediated endocytosis. Upon GTP hydrolysis, dynamin constricts a lipid bilayer. Previously, a three-dimensional structure of mutant dynamin in the constricted state was determined by helical reconstruction methods. We solved the nonconstricted state by a single-particle approach and show that the stalk region of dynamin undergoes a large conformational change that drives tube constriction.
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