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- Publisher
- Springer Journals
- Copyright
- Copyright © 1999 by Macmillan Magazines Ltd.
- Subject
- Life Sciences; Life Sciences, general; Cell Biology; Cancer Research; Developmental Biology; Stem Cells
- ISSN
- 1465-7392
- eISSN
- 1476-4679
- DOI
- 10.1038/8997
- Publisher site
- See Article on Publisher Site
Abstract
The GTPase dynamin plays an essential part in endocytosis by catalysing the fission of nascent clathrin-coated vesicles from the plasma membrane. Using preformed phosphatidylinositol-4,5-bisphosphate-containing lipid nanotubes as a membrane template for dynamin self-assembly, we investigate the conformational changes that arise during GTP hydrolysis by dynamin. Electron microscopy reveals that, in the GTP-bound state, dynamin rings appear to be tightly packed together. After GTP hydrolysis, the spacing between rings increases nearly twofold. When bound to the nanotubes, dynamin"s GTPase activity is cooperative and is increased by three orders of magnitude compared with the activity of unbound dynamin. An increase in the k cat (but not the K m) of GTP hydrolysis accounts for the pronounced cooperativity. These data indicate that a novel, lengthwise (‘spring-like’) conformational change in a dynamin helix may participate in vesicle fission.
Journal
Nature Cell Biology – Springer Journals
Published: May 1, 1999