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J Biol Chem, Vol. 273, Issue 33, 20894-20902, August 14, 1998

Kinetic Analysis of the Interaction of Actin-depolymerizing Factor (ADF)/Cofilin with G- and F-Actins
COMPARISON OF PLANT AND HUMAN ADFs AND EFFECT OF PHOSPHORYLATION

Fariza Ressad, Dominique Didry, Gui-Xian Xia^§, Yan Hong^§, Nam-Hai Chua^¶, Dominique Pantaloni, and Marie-France Carlier

From the  Dynamique du Cytosquelette, Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France, the ^§ Laboratory of Plant Cell Biology, Institute of Molecular Agrobiology, National University of Singapore, Singapore 118240, and the ^¶ Laboratory of Plant Molecular Biology, Rockefeller University, New York, New York 10021

The thermodynamics and kinetics of actin interaction with Arabidopsis thaliana actin-depolymerizing factor (ADF)₁, human ADF, and S6D mutant ADF₁ protein mimicking phosphorylated (inactive) ADF are examined comparatively. ADFs interact with ADP·G-actin in rapid equilibrium (k₊ = 155 µM¹·s¹ and k = 16 s¹ at 4 °C under physiological ionic conditions). The kinetics of interaction of plant and human ADFs with F-actin are slower and exhibit kinetic cooperativity, consistent with a scheme in which the initial binding of ADF to two adjacent subunits of the filament nucleates a structural change that propagates along the filament, allowing faster binding of ADF in a "zipper" mode. ADF binds in a non-cooperative faster process to gelsolin-capped filaments or to subtilisin-cleaved F-actin, which are structurally different from standard filaments (Orlova, A., Prochniewicz, E., and Egelman, E. H. (1995) J. Mol. Biol. 245, 598-607). In contrast, the binding of phalloidin to F-actin cooperatively inhibits its interaction with ADF. The ADF-facilitated nucleation of ADP·actin self-assembly indicates that ADF stabilizes lateral interactions in the filament. Plant and human ADFs cause only partial depolymerization of F-actin at pH 8, consistent with identical functions in enhancing F-actin dynamics. Phosphorylation does not affect ADF activity per se, but decreases its affinity for actin by 20-fold.

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