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Membrane depolarization induces the undulating phosphorylation/dephosphorylation of glycogen synthase kinase 3beta, and this dephosphorylation involves protein phosphatases 2A and 2B in SH-SY5Y human neuroblastoma cells

Cited 52 time in Web of Science Cited 51 time in Scopus
Authors

Lee, Yun-Il; Seo, MiRan; Kim, Yeni; Kim, So-Young; Kang, Ung Gu; Kim, Yong-Sik; Juhnn, Yong-Sung

Issue Date
2005-04-01
Publisher
American Society for Biochemistry and Molecular Biology
Citation
J Biol Chem. 2005 Jun 10;280(23):22044-52. Epub 2005 Mar 30.
Keywords
Androstadienes/pharmacologyAnimalsCalcineurin/*chemistryCalcium/metabolismCell LineCell Line, TumorCell Membrane/*metabolismEnzyme Inhibitors/pharmacologyGlioblastoma/metabolismGlycogen Synthase Kinase 3/*metabolismHippocampus/cytology/metabolismHumansImmunoblottingImmunoprecipitationMicroscopy, ConfocalNaphthalenes/pharmacologyPC12 CellsPhosphoprotein Phosphatases/*chemistryPhosphorylationPotassium Chloride/pharmacologyRatsSerine/chemistryThreonine/chemistryTime FactorsTransfection
Abstract
Changes in plasma membrane electrical potential evoke signals that regulate the expressions of various genes in the nervous system. However, the role of glycogen synthase kinase 3beta (GSK-3beta) in this process has not been elucidated. Thus, this study was performed to examine whether membrane depolarization can regulate the phosphorylation of GSK-3beta and to identify the molecular mechanisms involved in this regulation. The depolarization by treating with 100 mm KCl for 5 min resulted in the undulating phosphorylation of GSK-3beta at Ser-9 in SH-SY5Y human neuroblastoma cells, in H19 -7/IGF-IR rat embryonic hippocampal cells, and in PC12 rat pheochromocytoma cells, but not in A172 human glioblastoma cells. Cellular beta-catenin contents showed a temporal pattern similar to that of the Ser-9 phosphorylation of GSK-3beta. Treatment with wortmannin or calphostin C or the expression of dominant negative Akt inhibited phosphorylation of GSK-3beta at Ser-9 following the KCl-induced depolarization of SH-SY5Y cells. Moreover, pretreatment with okadaic acid or cyclosporin A blocked the dephosphorylation of GSK-3beta at Ser-9 at 0, 15, and 30 min after KCl-induced depolarization, and the activity of protein phosphatases (PP) 2A and 2B increased at these times. Treatment with nifedipine or calcium-free medium inhibited GSK-3beta dephosphorylation following membrane depolarization, and the amounts of co-immunoprecipitated GSK-3beta and PP2A changed in parallel with GSK-3beta dephosphorylation. Our study demonstrated that KCl-induced depolarization caused undulating GSK-3beta phosphorylation/dephosphorylation, which was regulated for the most part by phosphatidylinositol 3-kinase and Akt (phosphorylation) and PP2A and PP2B (dephosphorylation), respectively.
ISSN
0021-9258 (Print)
Language
English
URI
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15799972

https://hdl.handle.net/10371/29637
DOI
https://doi.org/10.1074/jbc.M413987200
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College of Medicine/School of Medicine (의과대학/대학원)Dept. of Biochemistry & Molecular Biology (생화학교실)Journal Papers (저널논문_생화학교실)
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