Cytochalasin D acts as an inhibitor of the actin-cofilin interaction

Biochem Biophys Res Commun. 2012 Jul 20;424(1):52-7. doi: 10.1016/j.bbrc.2012.06.063. Epub 2012 Jun 20.


Cofilin, a key regulator of actin filament dynamics, binds to G- and F-actin and promotes actin filament turnover by stimulating depolymerization and severance of actin filaments. In this study, cytochalasin D (CytoD), a widely used inhibitor of actin dynamics, was found to act as an inhibitor of the G-actin-cofilin interaction by binding to G-actin. CytoD also inhibited the binding of cofilin to F-actin and decreased the rate of both actin polymerization and depolymerization in living cells. CytoD altered cellular F-actin organization but did not induce net actin polymerization or depolymerization. These results suggest that CytoD inhibits actin filament dynamics in cells via multiple mechanisms, including the well-known barbed-end capping mechanism and as shown in this study, the inhibition of G- and F-actin binding to cofilin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / drug effects*
  • Actin Depolymerizing Factors / antagonists & inhibitors*
  • Actin Depolymerizing Factors / metabolism
  • Actins / antagonists & inhibitors*
  • Actins / metabolism
  • Animals
  • COS Cells
  • Chlorocebus aethiops
  • Cytochalasin D / pharmacology*


  • Actin Depolymerizing Factors
  • Actins
  • Cytochalasin D