Fig. S7.

Recruitment of ForG-N is PIP₃- but not Arp2/3 complex-dependent. Vegetative WT cells expressing YFP–ForG-N were seeded on glass-bottom dishes in low-osmolarity phosphate buffer and imaged either in the absence or presence of the inhibitors indicated. Notably, treatment of cells with the PIP₃ kinase inhibitor LY2904002 at 25 μM or 50 μM was sufficient to delocalize ForG-N completely from the membrane and render it entirely cytosolic, supporting the view that PIP₃, together with Ras signaling, is required for ForG targeting (also Fig. 6E). By contrast, treatment with the Arp2/3 complex inhibitor CK666 showed no significant effect at 50 μM and 100 μM, indicating that ForG does not require the Arp2/3 complex for targeting to the cups (white stars). Confocal sections of live cells are shown. (Scale bar: 5 μm.)