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The stalk region of dynamin drives the constriction of dynamin tubes

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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Figure 1: Image analysis of dynamin lipid tubes.
Figure 2: Comparison of ΔPRD dynamin lipid tubes in nonconstricted and constricted states.

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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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Correspondence to Edward H Egelman.

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The authors declare no competing financial interests.

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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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