Cell adhesion, migration and the maintenance of cell polarity are all processes that depend on the correct targeting of integrins and the dynamic remodelling of integrin-containing adhesion sites. The importance of the endo/exocytic cycle of integrins as a key regulator of these functions is increasingly recognized. Several recent publications have provided mechanistic insight into how integrin traffic is regulated in cells. Increasing evidence suggests that small GTPases such as Arf6 and members of the Rab family control integrin internalization and recycling back to the plasma membrane along microtubules. The fine tuning of these trafficking events seems to be mediated by specific guanine-nucleotide-exchange factors (GEFs) and GTPase-activating proteins (GAPs). In addition, several kinases regulate integrin traffic. The identification of their substrates has demonstrated how these kinases regulate integrin traffic by controlling small GTPases or stabilizing cytoskeletal tracks that are crucial for efficient traffic of integrins to the plasma membrane.