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Published 12 September 2005. doi:10.1083/jcb.200504156
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 170, Number 6, 889-893
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 A novel mechanism of actin filament processive capping by formin : solution of the rotation paradox



Tom Shemesh1, Takanori Otomo2, Michael K. Rosen2, Alexander D. Bershadsky3, and Michael M. Kozlov1

1 Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, 69978 Tel Aviv, Israel
2 Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75390
3 Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot 76100, Israel

Correspondence to Michael M. Kozlov: michk{at}post.tau.ac.il


Abstract
The FH2 domains of formin family proteins act as processive cappers of actin filaments. Previously suggested stair-stepping mechanisms of processive capping imply that a formin cap rotates persistently in one direction with respect to the filament. This challenges the formin-mediated mechanism of intracellular cable formation. We suggest a novel scenario of processive capping that is driven by developing and relaxing torsion elastic stresses. Based on the recently discovered crystal structure of an FH2–actin complex, we propose a second mode of processive capping—the screw mode. Within the screw mode, the formin dimer rotates with respect to the actin filament in the direction opposite to that generated by the stair-stepping mode so that a combination of the two modes prevents persistent torsion strain accumulation. We determine an optimal regime of processive capping, whose essence is a periodic switch between the stair-stepping and screw modes. In this regime, elastic energy does not exceed feasible values, and supercoiling of actin filaments is prevented.

Abbreviation used in this paper: NEM, N-ethylmaleimide.


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