Actin polymerization drives membrane movement and is spatially
regulated by membrane-associated signaling complexes. Rho-family
GTPases (such as Rac and Cdc42) bind and activate actin nucleation
factors, which localize to discrete zones--- along the membrane
corresponding to sites of actin polymerization and membrane
protrusions. However, it is unclear how actin networks spatially organize
signaling proteins into clusters and how this spatial organization affects
signal transduction. By reconstituting a Cdc42-driven signaling cascade
from purified proteins and supported lipid bilayers, we have gained
mechanistic insights into how actin dynamics exert local feedback control
on signal transduction events at the membrane.