RhoA stimulates cell contractility by recruiting downstream effectors to the cortical plasma membrane. We now show that direct binding by anillin is required for effective signaling: this antagonizes the otherwise labile membrane association of GTP-RhoA to promote effector recruitment. However， since its binding to RhoA blocks access by other effectors， we demonstrate that anillin must also concentrate membrane phosphoinositide-4，5-P (PIP) to promote signaling. We propose and test a sequential pathway where GTP-RhoA first binds to anillin and then is retained at the membrane by PIP after it disengages from anillin. Importantly， re-binding of membrane GTP-RhoA to anillin， regulated by the cortical density of anillin， creates cycles through this pathway. These cycles repeatedly reset the dissociation kinetics of GTP-RhoA， substantially increasing its dwell time to recruit effectors. Thus， anillin regulates RhoA signaling by a paradigm of kinetic scaffolding that may apply to other signals whose efficacy depends on their cortical dwell times.