Abstract
Plant actin depolymerizing factor (ADF) binds to both monomeric and filamentous actin, and plays a key role in the organization of the actin cytoskeleton. In this issue, Dong et al. (pp. 250–261) demonstrate that charged residues Arg98 and Lys100 of ADF1 are essential for both G‐ and F‐actin binding, and that basic residues on β‐strand 5 (K82/A) and α‐helix 4 (R135/A, R137/A) form another actin binding site for F‐actin.
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