Rho GTPase family proteins have a well-characterised role in regulating cell migration and adhesion dynamics, but the mechanisms by which guanine nucleotide exchange factors (GEFs) regulate their activity are less well understood. Asef2 is a recently identified GEF that has been shown to act on Rac and Cdc42; on page 4535, Donna Webb and colleagues now characterise cellular roles for Asef2. They first confirm that Asef2 increases cellular levels of active Rac and Cdc42; in addition, they show that Asef2 decreases the level of active RhoA. Similarly to the GTPases that it regulates, Asef2 is seen to localise at the leading edge of cells, where actin-based protrusions that enable cell migration form. When Asef2 is overexpressed, both the velocity of cell migration and the rate of adhesion turnover significantly increases. However, the authors find that these Asef2-mediated effects depend on Rac and not on Cdc42, at least in the HT1080 cell line used in this study. Furthermore, decreased RhoA activity is also required for Asef2 to mediate its effects on cell migration. Finally, the authors show that PI3K and Akt are both involved in Asef2-mediated regulation of cell migration and adhesion turnover, probably downstream of Rac activation. Therefore, the authors conclude, Asef2 coordinately regulates Rac and RhoA activity to promote cell migration and adhesion turnover through a pathway involving PI3K and Akt.