Translocation of vesicles containing the glucose transporter GLUT4 to the surface of fat and muscle cells is an important part of the body's response to insulin. The signalling pathway involved hinges on phosphoinositide 3-kinase (PI3K) and its downstream kinase PKB (also known as Akt); however, the key PKB targets have remained elusive. Jeremy Tavaré and coworkers now unveil one of these: PIKfyve, an enzyme that generates the phospholipid PtdIns(3,5)P2 from PtdIns(3)P (see p. 5985). Identifying PIKfyve as a protein that is phosphorylated in cells stimulated by insulin, the authors show that it is phosphorylated on Ser318 by PKB in vitro and that this increases its activity. They then demonstrate that the PI3K inhibitor wortmannin can block insulin-induced phosphorylation of Ser318 in vivo. Finally, they show that PIKfyve colocalizes with a marker for GLUT4-containing vesicles and can modulate insulin-dependent trafficking of vesicles containing this marker. Their findings thus indicate that PIKfyve is a PKB effector in insulin signalling. However, since it has previously been implicated in endosomal sorting and PKB responds to numerous extracellular stimuli, PIKfyve could have a wider role in signal-regulated membrane trafficking.