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J Mol Biol. 2008 Sep 5;381(3):550-8. doi: 10.1016/j.jmb.2008.05.055. Epub 2008 May 29.

Cofilin increases the bending flexibility of actin filaments: implications for severing and cell mechanics.

Author information

1
Yale University, Department of Molecular Biophysics and Biochemistry, 260 Whitney Avenue, New Haven, CT 06520, USA.

Abstract

We determined the flexural (bending) rigidities of actin and cofilactin filaments from a cosine correlation function analysis of their thermally driven, two-dimensional fluctuations in shape. The persistence length of actin filaments is 9.8 microm, corresponding to a flexural rigidity of 0.040 pN microm(2). Cofilin binding lowers the persistence length approximately 5-fold to a value of 2.2 microm and the filament flexural rigidity to 0.0091 pN microm(2). That cofilin-decorated filaments are more flexible than native filaments despite an increased mass indicates that cofilin binding weakens and redistributes stabilizing subunit interactions of filaments. We favor a mechanism in which the increased flexibility of cofilin-decorated filaments results from the linked dissociation of filament-stabilizing ions and reorganization of actin subdomain 2 and as a consequence promotes severing due to a mechanical asymmetry. Knowledge of the effects of cofilin on actin filament bending mechanics, together with our previous analysis of torsional stiffness, provide a quantitative measure of the mechanical changes in actin filaments associated with cofilin binding, and suggest that the overall mechanical and force-producing properties of cells can be modulated by cofilin activity.

PMID:
18617188
PMCID:
PMC2753234
DOI:
10.1016/j.jmb.2008.05.055
[Indexed for MEDLINE]
Free PMC Article

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