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The stalk region of dynamin drives the constriction of dynamin tubes

Nature Structural & Molecular Biology volume 11, pages 574–575 (2004)Cite this article

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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Authors and Affiliations

  1. Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia, USA

    Yen-Ju Chen & Edward H Egelman

  2. 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

Authors
  1. Yen-Ju Chen
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  2. Peijun Zhang
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  3. Edward H Egelman
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  4. Jenny E Hinshaw
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Correspondence to Edward 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

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