J. Cell Biol.
© The Rockefeller University Press
0021-9525/97/08/771/11 $2.00
Volume 138, Number 4, August 25, 1997 771-781

Cofilin Changes the Twist of F-Actin: Implications for Actin Filament Dynamics and Cellular Function

Amy McGough,^* Brian Pope, Wah Chiu,^* and Alan Weeds

^* Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030; and  Medical Research Council Laboratory of Molecular Biology, Cambridge, CB2 2QH, United Kingdom

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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