title: Dynamin: membrane scission meets physics.
abstract: Dynamin hydrolyzes GTP to constrict and sever membranes. Experimental advances bring dynamin into the realm of physics and reveal key roles for membrane tension and bending at the edge of the constriction.
authors.affiliation: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. james.hurley@nih.gov
authors.forename: James H
authors.initials: JH
authors.lastname: Hurley
authors.forename: Jenny E
authors.initials: JE
authors.lastname: Hinshaw
mesh_terms: D002462:Cell Membrane / Q000378:metabolism; D020285:Cryoelectron Microscopy; D034281:Dynamins / Q000378:metabolism* / Q000648:ultrastructure; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy
chemical_list: D006160:Guanosine Triphosphate; D034281:Dynamins