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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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
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DOI: https://doi.org/10.1038/nsmb762
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