During cell adhesion and migration, focal adhesions (FAs) form and dissolve, and cytoplasmic actin structures such as filopodia and lamellipodia are dynamically reorganised. These processes must be spatially and temporally coordinated – but how is this controlled? On page 3071, Bruce Mayer and colleagues describe a role for the PxxP motifs of the non-receptor tyrosine kinase Abl – which is known to modulate actin rearrangement – in the coordination of actin dynamics and FA formation. The authors show that the four PxxP motifs (which bind to SH3 domains) are required for the formation of filopodia during cell attachment. Using an SH3-domain phage-display library, they show that the Crk and Nck families of adaptor proteins are preferential binding partners of Abl. Overexpression of Nck proteins increases the number of filopodia per cell and downregulates FAs; by contrast, cells that overexpress Crk proteins have fewer filopodia, spread more quickly and upregulate the formation of FAs and lamellipodia. The authors propose a model in which binding to Abl PxxP motifs downregulates signalling through Crk proteins and stimulates Nck signalling, both of which favour filopodia over lamellipodia. They conclude that, through Crk and Nck, Abl coordinates FA formation and actin reorganisation.