Nature 388, 78–82 (1997)

Figure 3a of this Letter was incomplete as published, with two curves being omitted as a result of an error in the reproduction process. The correct is shown here.

Figure 3: The effects of cofilin mutations on actin-filament depolymerization in vivo and in vitro.
figure 1

a, The percentage of cells with visible actin-filament structures in wild-type, cof1–5 and cof1–22 cells at different times after the addition of Lat-A at 25 °C was quantified by rhodamine–phalloidin staining and fluorescent microscopy. For each strain and time point, at least 200 cells from two independent experiments were scored for the presence of actin patches. b, The F-actin depolymerization stimulated by recombinant wild-type, Cof1–5 and Cof1–22 cofilin was followed by the decrease in light-scattering at 400 nm. Note that dilution of 5 μM yeast actin filaments to 0.5 μM in the absence of cofilin results in slow actin-filament depolymerization. Wild-type cofilin and Cof1–5 cause large increases in the rates of depolymerization, whereas recombinant Cof1–22 causes only a small increase in actin-filament depolymerization rates. The cofilin and yeast actin samples used in these experiments were more than 99% and 95% pure, respectively, based on Coomassie-stained SDS gels (data not shown).

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