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Chronophin activation is necessary in Doxorubicin-induced actin cytoskeleton alteration.


ABSTRACT: Although doxorubicin (Dox)-induced oxidative stress is known to be associated with cytotoxicity, the precise mechanism remains unclear. Genotoxic stress not only generates free radicals, but also affects actin cytoskeleton stability. We showed that Dox-induced RhoA signaling stimulated actin cytoskeleton alterations, resulting in central stress fiber disruption at early time points and cell periphery cortical actin formation at a later stage, in HeLa cells. Interestingly, activation of a cofilin phosphatase, chronophin (CIN), was initially evoked by Dox-induced RhoA signaling, resulting in a rapid phosphorylated cofilin turnover leading to actin cytoskeleton remodeling. In addition, a novel interaction between CIN and 14-3-3? was detected in the absence of Dox treatment. We demonstrated that CIN activity is quite contrary to 14-3-3? binding, and the interaction leads to enhanced phosphorylated cofilin levels. Therefore, initial CIN activation regulation could be critical in Dox-induced actin cytoskeleton remodeling through RhoA/cofilin signaling. [BMB Reports 2017; 50(6): 335-340].

SUBMITTER: Lee SJ 

PROVIDER: S-EPMC5498145 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

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Chronophin activation is necessary in Doxorubicin-induced actin cytoskeleton alteration.

Lee Su Jin SJ   Park Jeen Woo JW   Kang Beom Sik BS   Lee Dong-Seok DS   Lee Hyun-Shik HS   Choi Sooyoung S   Kwon Oh-Shin OS  

BMB reports 20170601 6


Although doxorubicin (Dox)-induced oxidative stress is known to be associated with cytotoxicity, the precise mechanism remains unclear. Genotoxic stress not only generates free radicals, but also affects actin cytoskeleton stability. We showed that Dox-induced RhoA signaling stimulated actin cytoskeleton alterations, resulting in central stress fiber disruption at early time points and cell periphery cortical actin formation at a later stage, in HeLa cells. Interestingly, activation of a cofilin  ...[more]

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