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The stalk region of dynamin drives the constriction of dynamin tubes
Author(s): Chen YJ, Zhang PJ, Egelman EH, Hinshaw JE
Source: NATURE STRUCTURAL & MOLECULAR BIOLOGY    Volume: 11    Issue: 6    Pages: 574-575    Published: JUN 2004  
Times Cited: 47     References: 12     
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.
Document Type: Article
Language: English
Reprint Address: Egelman, EH (reprint author), Univ Virginia, Dept Biochem & Mol Genet, Charlottesville, VA USA
Addresses:
1. Univ Virginia, Dept Biochem & Mol Genet, Charlottesville, VA USA
2. NIDDKD, Lab Cell Biochem & Biol, NIH, Bethesda, MD 20892 USA
Publisher: NATURE PUBLISHING GROUP, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 USA
Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology
IDS Number: 824DO
ISSN: 1545-9985
DOI: 10.1038/nsmb762
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