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

Kazuyasu Shoji, Kazumasa Ohashi, Kaori Sampei, Masato Oikawa, Kensaku Mizuno

    Research output: Contribution to journalArticlepeer-review

    55 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)52-57
    Number of pages6
    JournalBiochemical and biophysical research communications
    Issue number1
    Publication statusPublished - 2012 Jul 20


    • Actin dynamics
    • Bimolecular fluorescence complementation (BiFC)
    • Cofilin
    • Cytochalasin D
    • Inhibitor
    • Protein-protein interaction

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology


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