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 complex. The physical mechanism of force generation by actin polymerization has been described theoretically using various approaches, but lacks support from experimental data. By the use of reconstituted motility medium, we find that the Wiskott Aldrich syndrome protein (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' Listeria. 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.

The dimeric (gemini) surfactant 12-2-12 (dimethylene-1,2-bis(dodecyl dimethylammonium bromide)) has been known to form threadlike micelles at relatively low concentrations. We investigated the micellar growth of this surfactant in aqueous solutions by the much-improved cryo-TEM technique (transmission electron microscopy at cryogenic temperature) in the concentration range between 0.26 and 1.5 wt %. The digitally acquired electron micrographs of solutions, with concentrations up to about 1 wt %, show the coexistence of spheroidal micelles and long, threadlike micelles, the number and length of the latter increasing with concentration at the expense of the former. The micrographs show very few elongated micelles of intermediate sizes. Also, the endcaps of the elongated micelles can be seen to be of a larger diameter than the cylindrical body of those micelles. These results lend support to the theories, developed by various workers, that predicted these features. Some branching is observed at a surfactant concentration of 0.62 wt %. Above 1 wt %, the elongated micelles show frequent branching. The electron micrographs of the 1.5 wt % solution have the appearance of the saturated network postulated by theory.

The actin cytoskeleton is an active gel which constantly remodels during cellular processes such as motility and division. Myosin II molecular motors are involved in this active remodeling process and therefore control the dynamic self-organization of cytoskeletal structures. Due to the complexity of in vivo systems, it is hard to investigate the role of myosin II in the reorganization process which determines the resulting cytoskeletal structures. Here we use an in vitro model system to show that myosin II actively reorganizes actin into a variety of mesoscopic patterns, but only in the presence of bundling proteins. We find that the nature of the reorganization process is complex, exhibiting patterns and dynamical phenomena not predicted by current theoretical models and not observed in corresponding passive systems (excluding motors). This system generates active networks, asters and even rings depending on motor and bundling protein concentrations. Furthermore, the motors generate the formation of the patterns, but above a critical concentration they can also disassemble them and even totally prevent the polymerization and bundling of actin filaments. These results may suggest that tuning the assembly and disassembly of cytoskeletal structures can be obtained by tuning the local myosin II concentration/activity.