In cells, actin polymerization at the plasma membrane is induced by the recruitment of proteins such as the Arp2/3 complex, and the zyxin/VASP complex1,2,3. The physical mechanism of force generation by actin polymerization has been described theoretically using various approaches4,5,6, but lacks support from experimental data. By the use of reconstituted motility medium7, we find that the Wiskott–Aldrich syndrome protein8,9 (WASP) subdomain, known as VCA, is sufficient to induce actin polymerization and movement when grafted on microspheres. Changes in the surface density of VCA protein or in the microsphere diameter markedly affect the velocity regime, shifting from a continuous to a jerky movement resembling that of the mutated ‘hopping’ Listeria10. These results highlight how simple physical parameters such as surface geometry and protein density directly affect spatially controlled actin polymerization, and play a fundamental role in actin-dependent movement.
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We thank J. Plastino for discussions and the purification of VCA proteins, and F. Castellano and P. Chavrier for the gift of the plasmid encoding VCA. Theoretical discussions were conducted by J. Prost. We thank D. Didry for the purification of Arp2/3, ADF-cofilin, and actin, and R. Boujemaa for the purification of the capping protein. We thank H. Boukellal for help in determining the VCA concentration on the beads, E. Paluch for helping in analysing the videos and K. Sekimoto and D. Pantaloni for discussions.
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Cell Chemical Biology (2019)
Advanced Biosystems (2019)
Physical Biology (2018)