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Fig. 9. The DAD/WH2 of INF2 binds the DID region. (A) Fluorescence anisotropy measurements using fluorescein-labeled INF2-(C) at 20 nM and increasing concentrations of INF2-(DID) reveals an apparent dissociation constant (K_d^app) of 1.1 µM (circles). The fluorescently labeled INF2-(C)-W mutant displays no measurable affinity for DID (squares). Similar results obtained in two independent experiments. (B) INF2-(DID) inhibits INF2-(FH1-FH2-C)-mediated depolymerization, but not polymerization. Pyrene-actin polymerization assays with 1 µM rabbit muscle actin monomers (5% pyrene labeled) and 300 nM of INF2-(FH1-FH2-C) in the absence or presence of 100 µM DID. In independent experiments, this concentration of INF2-(DID) has no effect on actin dynamics. (C) Inhibition of INF2-(FH1-FH2-C)-mediated depolymerization by DID. Actin monomers (1.05 µM, 5% pyrene labeled) were polymerized for 16 hours at 23°C in polymerization buffer, then diluted to 1 µM in the same buffer containing 250 nM INF2-(FH1-FH2-C) and varying concentrations of INF2-(DID). Filament depolymerization was measured by the decrease in pyrene fluorescence intensity with time. F1F2C, INF2-(FH1-FH2-C); D, INF2-(DID).

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