Reconstitution of actin-based motility by vasodilator-stimulated phosphoprotein (VASP) depends on the recruitment of F-actin seeds from the solution produced by cofilin.

ABSTRACT: Vasodilator-stimulated phosphoprotein (VASP) is active in many filopodium-based and cytoskeleton reorganization processes. It is not fully understood how VASP directly functions in actin-based motility and how regulatory proteins affect its function. Here, we combine bead motility assay and single filament experiments. In the presence of a bundling component, actin bundles that grow from the surface of WT-VASP-coated beads induced movement of the beads. VASP promotes actin-based movement alone, in the absence of other actin nucleators. We propose that at physiological salt conditions VASP nucleation activity is too weak to promote motility and bundle formation. Rather, VASP recruits F-actin seeds from the solution and promotes their elongation. Cofilin has a crucial role in the nucleation

SUBMITTER: Siton O 

PROVIDER: S-EPMC4223328 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature