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Cofilin phosphorylation is elevated after F ‐actin disassembly induced by R ac1 depletion
Author(s) -
Liu Linna,
Li Jing,
Zhang Liwang,
Zhang Feng,
Zhang Rong,
Chen Xiang,
Brakebusch Cord,
Wang Zhipeng,
Liu Xinyou
Publication year - 2015
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.1235
Subject(s) - cofilin , microbiology and biotechnology , rac1 , phosphorylation , actin remodeling , actin , actin remodeling of neurons , mdia1 , cytoskeleton , actin cytoskeleton , biology , chemistry , signal transduction , biochemistry , cell
Cytoskeletal reorganization is essential to keratinocyte function. Rac1 regulates cytoskeletal reorganization through signaling pathways such as the cofilin cascade. Cofilin severs actin filaments after activation by dephosphorylation. Rac1 was knocked out in mouse keratinocytes and it was found that actin filaments disassembled. In the epidermis of mice in which Rac1 was knocked out only in keratinocytes, cofilin phosphorylation was aberrantly elevated, corresponding to repression of the phosphatase slingshot1 (SSH1). These effects were independent of the signaling pathways for p21‐activated kinase/LIM kinase (Pak/LIMK), protein kinase C, or protein kinase D or generation of reactive oxygen species. Similarly, when actin polymerization was specifically inhibited or Rac1 was knocked down, cofilin phosphorylation was enhanced and SSH1 was repressed. Repression of SSH1 partially blocked actin depolymerization induced by Rac1 depletion. Therefore, aberrant cofilin phosphorylation that induces actin polymerization might be a consequence of actin disassembly induced by the absence of Rac1. © 2015 BioFactors, 41(5):352–359, 2015