Relaxing the actin cytoskeleton for adhesion and movement with Ena/VASP.
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.
Trichet
Léa
L
Laboratoire Matière et Systèmes Complexes, Centre National de la Recherche Scientifique, Paris 7, 75205 Paris Cedex 13, France.
Sykes
Cécile
C
Plastino
Julie
J
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
D051376:Actin-Related Protein 2-3 Complex; D000199:Actins; D004268:DNA-Binding Proteins; C092744:ENA-VASP proteins