These authors contributed equally to this work.
Direct dynamin–actin interactions regulate the actin cytoskeleton
Article first published online: 8 OCT 2010
Copyright © 2010 European Molecular Biology Organization
The EMBO Journal
Volume 29, Issue 21, pages 3593–3606, November 3, 2010
How to Cite
Gu, C., Yaddanapudi, S., Weins, A., Osborn, T., Reiser, J., Pollak, M., Hartwig, J. and Sever, S. (2010), Direct dynamin–actin interactions regulate the actin cytoskeleton. The EMBO Journal, 29: 3593–3606. doi: 10.1038/emboj.2010.249
There is a Have you seen ...? (November 2010) associated with this Article.
- Issue published online: 3 NOV 2010
- Article first published online: 8 OCT 2010
- Manuscript Accepted: 10 SEP 2010
- Manuscript Received: 10 MAY 2010
The large GTPase dynamin assembles into higher order structures that are thought to promote endocytosis. Dynamin also regulates the actin cytoskeleton through an unknown, GTPase-dependent mechanism. Here, we identify a highly conserved site in dynamin that binds directly to actin filaments and aligns them into bundles. Point mutations in the actin-binding domain cause aberrant membrane ruffling and defective actin stress fibre formation in cells. Short actin filaments promote dynamin assembly into higher order structures, which in turn efficiently release the actin-capping protein (CP) gelsolin from barbed actin ends in vitro, allowing for elongation of actin filaments. Together, our results support a model in which assembled dynamin, generated through interactions with short actin filaments, promotes actin polymerization via displacement of actin-CPs.