Publications
Detailed Information
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
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Yun-Il | - |
dc.contributor.author | Seo, MiRan | - |
dc.contributor.author | Kim, Yeni | - |
dc.contributor.author | Kim, So-Young | - |
dc.contributor.author | Kang, Ung Gu | - |
dc.contributor.author | Kim, Yong-Sik | - |
dc.contributor.author | Juhnn, Yong-Sung | - |
dc.date.accessioned | 2010-07-08 | - |
dc.date.available | 2010-07-08 | - |
dc.date.issued | 2005-04-01 | - |
dc.identifier.citation | J Biol Chem. 280(23), 22044-22052 | en |
dc.identifier.issn | 0021-9258 (Print) | - |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15799972 | - |
dc.identifier.uri | https://hdl.handle.net/10371/68487 | - |
dc.description.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. | en |
dc.language.iso | en | en |
dc.publisher | American Society for Biochemistry and Molecular Biology | en |
dc.subject | Androstadienes/pharmacology | en |
dc.subject | Animals | en |
dc.subject | Calcineurin/*chemistry | en |
dc.subject | Calcium/metabolism | en |
dc.subject | Cell Line | en |
dc.subject | Cell Line, Tumor | en |
dc.subject | Cell Membrane/*metabolism | en |
dc.subject | Enzyme Inhibitors/pharmacology | en |
dc.subject | Glioblastoma/metabolism | en |
dc.subject | Glycogen Synthase Kinase 3/*metabolism | en |
dc.subject | Hippocampus/cytology/metabolism | en |
dc.subject | Humans | en |
dc.subject | Immunoblotting | en |
dc.subject | Immunoprecipitation | en |
dc.subject | Microscopy, Confocal | en |
dc.subject | Naphthalenes/pharmacology | en |
dc.subject | PC12 Cells | en |
dc.subject | Phosphoprotein Phosphatases/*chemistry | en |
dc.subject | Phosphorylation | en |
dc.subject | Potassium Chloride/pharmacology | en |
dc.subject | Rats | en |
dc.subject | Serine/chemistry | en |
dc.subject | Threonine/chemistry | en |
dc.subject | Time Factors | en |
dc.subject | Transfection | en |
dc.title | 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 | en |
dc.type | Article | en |
dc.contributor.AlternativeAuthor | 이윤일 | - |
dc.contributor.AlternativeAuthor | 서미란 | - |
dc.contributor.AlternativeAuthor | 김예니 | - |
dc.contributor.AlternativeAuthor | 김소영 | - |
dc.contributor.AlternativeAuthor | 강웅구 | - |
dc.contributor.AlternativeAuthor | 김용식 | - |
dc.contributor.AlternativeAuthor | 전용성 | - |
dc.identifier.doi | 10.1074/jbc.M413987200 | - |
- Appears in Collections:
- Files in This Item:
- There are no files associated with this item.
Item View & Download Count
Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.