Cofilin Increases the Bending Flexibility of Actin Filaments: Implications for Severing and Cell Mechanics

Brannon R McCullough, Laurent Blanchoin, Jean Louis Martiel, Enrique M. De La Cruz

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168 Scopus citations


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 μm, corresponding to a flexural rigidity of 0.040 pN μm2. Cofilin binding lowers the persistence length ∼5-fold to a value of 2.2 μm and the filament flexural rigidity to 0.0091 pN μm2. 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.

Original languageEnglish (US)
Pages (from-to)550-558
Number of pages9
JournalJournal of Molecular Biology
Issue number3
StatePublished - Sep 5 2008

Bibliographical note

Funding Information:
We thank Dr. Simon Mochrie (Yale University) for comments on the manuscript. This work was supported by grants from the American Heart Association (0655849T), National Science Foundation (MCB-0546353), and National Institutes of Health (GM071688) to E.M.D.L.C. B.R.M. is supported by National Institutes of Health training grant T32GM007223.


  • biopolymer mechanics
  • imaging
  • persistence length
  • severing
  • single molecule


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