  Self organization mechanisms are essential for the cytoskeleton to adapt to
the requirements of living cells. They rely on the intricate interplay of
cytoskeletal filaments, crosslinking proteins and molecular motors. Here we
present an in vitro minimal model system consisting of actin filaments, fascin
and myosin-II filaments exhibiting pulsative collective long range dynamics.
The reorganizations in the highly dynamic steady state of the active gel are
characterized by alternating periods of runs and stalls resulting in a
superdiffusive dynamics of the network's constituents. They are dominated by
the complex competition of crosslinking molecules and motor filaments in the
network: Collective dynamics are only observed if the relative strength of the
binding of myosin-II filaments to the actin network allows exerting high enough
forces to unbind actin/fascin crosslinks. The feedback between structure
formation and dynamics can be resolved by combining these experiments with
phenomenological simulations based on simple interaction rules.
