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|Title:||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||Authors:||Ressad, F.
|Issue Date:||14-Aug-1998||Citation:||Ressad, F., Didry, D., Xia, G.-X., Hong, Y., Chua, N.-H., Pantaloni, D., Carlier, M.-F. (1998-08-14). 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. Journal of Biological Chemistry 273 (33) : 20894-20902. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.273.33.20894||Abstract:||The thermodynamics and kinetics of actin interaction with Arabidopsis thaliana actin-depolymerizing factor (ADF) 1, human ADF, and S6D mutant ADF 1 protein mimicking phosphorylated (inactive) ADF are examined comparatively. ADFs interact with ADP-G-actin in rapid equilibrium (k + = 155 μM -1·s - 1 and k - = 16 s -1 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.||Source Title:||Journal of Biological Chemistry||URI:||http://scholarbank.nus.edu.sg/handle/10635/132754||ISSN:||00219258||DOI:||10.1074/jbc.273.33.20894|
|Appears in Collections:||Staff Publications|
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