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