The stalk region of dynamin drives the constriction of dynamin tubes (original) (raw)
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- Published: 09 May 2004
Nature Structural & Molecular Biology volume 11, pages 574–575 (2004)Cite this article
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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.
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Acknowledgements
We thank K.-H. Moon for his help with the helical hand determination. This work was supported by a grant from the US National Institute of Biomedical Imaging and Bioengineering, US National Institutes of Health, to E.H.E.
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Authors and Affiliations
- Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia, USA
Yen-Ju Chen & Edward H Egelman - Laboratory of Cell Biochemistry and Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA
Peijun Zhang & Jenny E Hinshaw
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- Yen-Ju Chen
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Correspondence toEdward H Egelman.
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Chen, YJ., Zhang, P., Egelman, E. et al. The stalk region of dynamin drives the constriction of dynamin tubes.Nat Struct Mol Biol 11, 574–575 (2004). https://doi.org/10.1038/nsmb762
- Received: 09 February 2004
- Accepted: 22 March 2004
- Published: 09 May 2004
- Issue Date: 01 June 2004
- DOI: https://doi.org/10.1038/nsmb762