title: Relaxing the actin cytoskeleton for adhesion and movement with Ena/VASP.
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.
authors: Laboratoire Matière et Systèmes Complexes, Centre National de la Recherche Scientifique, Paris 7, 75205 Paris Cedex 13, France.
authors: Léa
authors: L
authors: Trichet
authors: Cécile
authors: C
authors: Sykes
authors: Julie
authors: J
authors: Plastino
mesh_terms: D051376:Actin-Related Protein 2-3 Complex / Q000378:metabolism; D000199:Actins; D000818:Animals; D002448:Cell Adhesion; D003599:Cytoskeleton; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004330:Drosophila / Q000166:cytology* / Q000378:metabolism
chemical_list: D051376:Actin-Related Protein 2-3 Complex; D000199:Actins; D004268:DNA-Binding Proteins; C092744:ENA-VASP proteins