Please use this identifier to cite or link to this item:
|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|
|Source:||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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Mar 8, 2018
WEB OF SCIENCETM
checked on Feb 12, 2018
checked on Mar 12, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.