Actin polymerization serves as a membrane domain switch in model lipid bilayers.

The ability of cells to mount localized responses to external or internal stimuli is critically dependent on organization of lipids and proteins in the plasma membrane. Involvement of the actin cytoskeleton in membrane organization has been documented, but an active role for actin networks that directly links internal organization of the cytoskeleton with membrane organization has not yet been identified. Here we show that branched actin networks formed on model lipid membranes enriched with the lipid second messenger PIP(2) trigger both temporal and spatial rearrangement of membrane components. Using giant unilamellar vesicles able to separate into two coexisting liquid phases, we demonstrate that polymerization of dendritic actin networks on the membrane induces phase separation of initially homogenous vesicles. This switch-like behavior depends only on the PIP(2)-N-WASP link between the membrane and actin network, and we find that the presence of a preexisting actin network spatially biases the location of phase separation. These results show that dynamic, membrane-bound actin networks alone can control when and where membrane domains form and may actively contribute to membrane organization during cell signaling.