Please use this identifier to cite or link to this item: https://doi.org/10.1074/jbc.273.33.20894
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.
Didry, D.
Xia, G.-X. 
Hong, Y. 
Chua, N.-H.
Pantaloni, D.
Carlier, M.-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

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

141
checked on Nov 19, 2018

WEB OF SCIENCETM
Citations

144
checked on Oct 23, 2018

Page view(s)

12
checked on Nov 8, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.