Focal adhesions link the extracellular matrix with the actin cytoskeleton and mediate integrin-dependent signalling to allow the cell to move in response to external cues. They consist of structural components (i.e. talin, paxillin and vinculin) and signalling molecules. The recruitment of talin to focal adhesions is mediated by Rap1-GTP-interacting adaptor molecule (RIAM), whose depletion leads to defects in migration and invasion of melanoma cells; however, the underlying mechanisms leading to these defects are not well understood. On page 5338, Joaquin Teixidó and colleagues set out to investigate the involvement of RIAM in focal adhesion turnover and dynamics. They find that RIAM-knockout melanoma and breast cancer cells have bigger and more-stable focal adhesions, suggesting that disassembly focal adhesion is impaired in these cells. The authors also observe that, in these cells, RIAM seems to be required for integrin-dependent MEK–Erk1/2 activation. Importantly, when MEK is overexpressed, focal adhesion disassembly and, subsequently, cell invasion is restored. Taken together, these data indicate that integrin-mediated, RIAM-dependent MEK activation represents a key feedback event required for efficient focal adhesion disassembly, which might explain how RIAM impacts on cell migration and invasion.