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Molecular mechanism of cofilin dephosphorylation by ouabain
- Title
- Molecular mechanism of cofilin dephosphorylation by ouabain
- Authors
- Jung J.; Kim M.; Choi S.; Kim M.-J.; Suh J.-k.; Choi E.C.; Lee K.
- Ewha Authors
- 이경림
- SCOPUS Author ID
- 이경림
- Issue Date
- 2006
- Journal Title
- Cellular Signalling
- ISSN
- 0898-6568
- Citation
- Cellular Signalling vol. 18, no. 11, pp. 2033 - 2040
- Indexed
- SCI; SCIE; SCOPUS
- Document Type
- Article
- Abstract
- We previously reported that phosphorylated cofilin-triosephosphate isomerase (TPI) complex interacts with Na,K-ATPase and enhances the pump activity through the phosphorylation of cofilin via Rho-mediated signaling pathway. In this study, we tested the hypothesis that the dephosphorylation of cofilin may be induced through Na,K-ATPase inhibition by ouabain. The phosphorylation level of cofilin by ouabain which decreases in a time- and dose-dependent manner in various human cell lines, remains unchanged by pretreatment with Src inhibitor, PP2; epidermal growth factor receptor (EGFR) inhibitor, AG1478; Raf-1 kinase (Raf) inhibitor, GW5074; and ERK kinase (MEK) inhibitor, PD98059, and by transfection of Ras dominant negative mutant (RasN17). This suggests that ouabain dephosphorylates cofilin through the Src/EGFR/Ras/Raf/MEK pathway. Ouabain activates Ras/Raf/MEK pathway, but down-regulates Rho kinase (ROCK)/LIM kinase (LIMK)/cofilin pathway, implying that there may be a cross-talk by ouabain between the Ras/Raf/MEK and the ROCK/LIMK/cofilin pathways. Immunofluorescence and flow cytometry suggest that ouabain-induced active form of cofilin may be involved in cytoskeletal reorganization and cell volume regulation. Thus, these findings demonstrate a new molecular mechanism for the dephosphorylation of cofilin through the inhibition of Na,K-ATPase by ouabain. © 2006 Elsevier Inc. All rights reserved.
- DOI
- 10.1016/j.cellsig.2006.03.014
- Appears in Collections:
- 약학대학 > 약학과 > Journal papers
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