Abstract
Cofilin is an actin depolymerizing protein found widely distributed in animals and plants. We have used electron cryomicroscopy and helical reconstruction to identify its binding site on actin filaments. Cofilin binds filamentous (F)-actin cooperatively by bridging two longitudinally associated actin subunits. The binding site is centered axially at subdomain 2 of the lower actin subunit and radially at the cleft between subdomains 1 and 3 of the upper actin subunit. Our work has revealed a totally unexpected (and unique) property of cofilin, namely, its ability to change filament twist. As a consequence of this change in twist, filaments decorated with cofilin have much shorter ‘actin crossovers' (∼75% of those normally observed in F-actin structures). Although their binding sites are distinct, cofilin and phalloidin do not bind simultaneously to F-actin. This is the first demonstration of a protein that excludes another actin-binding molecule by changing filament twist. Alteration of F-actin structure by cofilin/ADF appears to be a novel mechanism through which the actin cytoskeleton may be regulated or remodeled.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 26, 2002, 12:47 p.m.) |
Deposited | 2 years, 1 month ago (July 22, 2023, 3:04 a.m.) |
Indexed | 1 day, 18 hours ago (Aug. 23, 2025, 12:58 a.m.) |
Issued | 27 years, 11 months ago (Aug. 25, 1997) |
Published | 27 years, 11 months ago (Aug. 25, 1997) |
Published Online | 27 years, 11 months ago (Aug. 25, 1997) |
Published Print | 27 years, 11 months ago (Aug. 25, 1997) |
@article{McGough_1997, title={Cofilin Changes the Twist of F-Actin: Implications for Actin Filament Dynamics and Cellular Function}, volume={138}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.138.4.771}, DOI={10.1083/jcb.138.4.771}, number={4}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={McGough, Amy and Pope, Brian and Chiu, Wah and Weeds, Alan}, year={1997}, month=aug, pages={771–781} }