To move, cells must simultaneously disassemble, reassemble and contract the actin cytoskeleton at different subcellular locations. So how do the signalling mechanisms involved ensure these compartmentalized responses? Gerald Burgstaller and Mario Gimona have approached this question by studying A7r5 cells, large vascular smooth muscle cells that have prominent actin cytoskeletons (see p. 223). In these cells, stimulation with phorbol ester induces actomyosin contraction in the cell body but motile responses (actin remodelling) in the cell periphery. The authors reveal that this is due to the existence of discrete actin microdomains at the periphery, in which contractility is locally inhibited. The microdomains are located at the interface between stress fibres and focal adhesions and contain structurally altered actin that cannot be stained with phalloidin. They specifically recruit cortactin - which stabilizes the actin-polymerizing machinery - and p190RhoGAP - which reduces contractility by antagonizing the GTPase RhoA. Moreover, they exclude myosin and hence the driving force for actomyosin contraction. Burgstaller and Gimona propose that the resultant local loss of contractility allows the turnover of focal adhesions and formation of podosomes necessary for successful cell migration, without affecting other parts of the actin cytoskeleton.