title: The stalk region of dynamin drives the constriction of dynamin tubes.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia, USA.
authors.forename: Yen-Ju
authors.initials: YJ
authors.lastname: Chen
authors.forename: Peijun
authors.initials: P
authors.lastname: Zhang
authors.forename: Edward H
authors.initials: EH
authors.lastname: Egelman
authors.forename: Jenny E
authors.initials: JE
authors.lastname: Hinshaw
mesh_terms: D034281:Dynamins / Q000737:chemistry* / Q000502:physiology / Q000648:ultrastructure; D008051:Lipid Bilayers; D008854:Microscopy, Electron; D020409:Molecular Motor Proteins; D011487:Protein Conformation
chemical_list: D008051:Lipid Bilayers; D020409:Molecular Motor Proteins; D034281:Dynamins