TY - JOUR
T1 - Cytochalasin D acts as an inhibitor of the actin-cofilin interaction
AU - Shoji, Kazuyasu
AU - Ohashi, Kazumasa
AU - Sampei, Kaori
AU - Oikawa, Masato
AU - Mizuno, Kensaku
N1 - Funding Information:
The SCADS inhibitor kit I and II (each consisting 95 chemical inhibitors) were provided by the Screening Committee of Anticancer Drugs through a Grant-in-Aid for Scientific Research on Priority Area ‘Cancer’ from the Ministry of Education, Culture, Sports, Science and Technology, Japan. Other chemical compounds (termed MO-1 to MO-768) had been synthesized as partial structures and analogs of natural products as well as enzyme inhibitors [25–27] .
PY - 2012/7/20
Y1 - 2012/7/20
N2 - 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.
AB - 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.
KW - Actin dynamics
KW - Bimolecular fluorescence complementation (BiFC)
KW - Cofilin
KW - Cytochalasin D
KW - Inhibitor
KW - Protein-protein interaction
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UR - http://www.scopus.com/inward/citedby.url?scp=84864081261&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2012.06.063
DO - 10.1016/j.bbrc.2012.06.063
M3 - Article
C2 - 22728040
AN - SCOPUS:84864081261
SN - 0006-291X
VL - 424
SP - 52
EP - 57
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -