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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
이경림scopus
Issue Date
2006
Journal Title
Cellular Signalling
ISSN
0898-6568JCR Link
Citation
vol. 18, no. 11, pp. 2033 - 2040
Indexed
SCI; SCIE; SCOPUS WOS scopus
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
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약학대학 > 약학과 > Journal papers
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