Relaxing the actin cytoskeleton for adhesion and movement with Ena/VASP
Open Access
- 31 March 2008
- journal article
- review article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 181 (1), 19-25
- https://doi.org/10.1083/jcb.200710168
Abstract
At cell–cell contacts, as well as at the leading edge of motile cells, the plasticity of actin structures is maintained, in part, through labile connections to the plasma membrane. Here we explain how and why Drosophila enabled/vasodilator stimulated phosphoprotein (Ena/VASP) proteins are candidates for driving this cytoskeleton modulation under the membrane.Keywords
This publication has 46 references indexed in Scilit:
- Cytoskeleton assembly at endothelial cell–cell contacts is regulated by αII-spectrin–VASP complexesThe Journal of cell biology, 2008
- C. elegans Enabled Exhibits Novel Interactions with N-WASP, Abl, and Cell-Cell JunctionsCurrent Biology, 2007
- Structural basis for the recruitment of profilin–actin complexes during filament elongation by Ena/VASPThe EMBO Journal, 2007
- Ena/VASP Proteins Have an Anti-Capping Independent Function in Filopodia FormationMolecular Biology of the Cell, 2007
- Enhanced EGFP-chromophore-assisted laser inactivation using deficient cells rescued with functional EGFP-fusion proteinsProceedings of the National Academy of Sciences of the United States of America, 2007
- Mechanism of Actin Network Attachment to Moving Membranes: Barbed End Capture by N-WASP WH2 DomainsCell, 2007
- VASP Governs Actin Dynamics by Modulating Filament AnchoringBiophysical Journal, 2007
- Organization of Actin Networks in Intact FilopodiaCurrent Biology, 2007
- The bundling activity of vasodilator-stimulated phosphoprotein is required for filopodium formationProceedings of the National Academy of Sciences of the United States of America, 2006
- How VASP enhances actin-based motilityThe Journal of cell biology, 2003