Cytochalasin D acts as an inhibitor of the actin-cofilin interaction.
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.
Department of Biomolecular Sciences, Graduate School of Life Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japan.
Kazuyasu
K
Shoji
Kazumasa
K
Ohashi
Kaori
K
Sampei
Masato
M
Oikawa
Kensaku
K
Mizuno
D008841:Actin Cytoskeleton / Q000187:drug effects*; D051339:Actin Depolymerizing Factors / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000199:Actins / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D019556:COS Cells; D002522:Chlorocebus aethiops; D015638:Cytochalasin D / Q000494:pharmacology*
D051339:Actin Depolymerizing Factors; D000199:Actins; D015638:Cytochalasin D