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Calcineurin dephosphorylates glycogen synthase kinase-3 beta at serine-9 in neuroblast-derived cells
DC Field | Value | Language |
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dc.contributor.author | Kim, Yeni | - |
dc.contributor.author | Lee, Yun-Il | - |
dc.contributor.author | Seo, MiRan | - |
dc.contributor.author | Kim, So-Young | - |
dc.contributor.author | Youn, Hong-Duk | - |
dc.contributor.author | Juhnn, Yong-Sung | - |
dc.contributor.author | Kim, Yong-Sik | - |
dc.contributor.author | Lee, Ji-Eun | - |
dc.date.accessioned | 2012-06-05T06:14:18Z | - |
dc.date.available | 2012-06-05T06:14:18Z | - |
dc.date.issued | 2009-10 | - |
dc.identifier.citation | JOURNAL OF NEUROCHEMISTRY; Vol.111 2; 344-354 | ko_KR |
dc.identifier.issn | 0022-3042 | - |
dc.identifier.uri | https://hdl.handle.net/10371/76857 | - |
dc.description.abstract | This study examined the role of calcineurin, a major calcium-dependent protein phosphatase, in dephosphorylating Ser-9 and activating glycogen synthase kinase-3 beta (GSK-3 beta). Treatment with calcineurin inhibitors increased phosphorylation of GSK-3 beta at Ser-9 in SH-SY5Y human neuroblastoma cells. The over-expression of a constitutively active calcineurin mutant, calcineurin A beta (1-401), led to a significant decrease in phosphorylation at Ser-9, an increase in the activity of GSK-3 beta, and an increase in the phosphorylation of tau. K(m) of calcineurin for a GSK-3 beta phosphopeptide was 469.3 mu M, and specific activity of calcineurin was 15.2 nmol/min/mg. In addition, calcineurin and GSK-3 beta were co-immunoprecipitated in neuron-derived cells and brain tissues, and calcineurin formed a complex only with dephosphorylated GSK-3 beta. We conclude that in vitro, calcineurin can dephosphorylate GSK-3 beta at Ser-9 and form a stable complex with GSK-3 beta, suggesting the possibility that calcineurin regulates the dephosphorylation and activation of GSK-3 beta in vivo. | ko_KR |
dc.language.iso | en | ko_KR |
dc.publisher | WILEY-BLACKWELL PUBLISHING, INC | ko_KR |
dc.subject | brain | ko_KR |
dc.subject | calcineurin | ko_KR |
dc.subject | dephosphorylation | ko_KR |
dc.subject | neuron-derived cells | ko_KR |
dc.subject | glycogen synthase kinase-3β | ko_KR |
dc.title | Calcineurin dephosphorylates glycogen synthase kinase-3 beta at serine-9 in neuroblast-derived cells | ko_KR |
dc.type | Article | ko_KR |
dc.contributor.AlternativeAuthor | 김예니 | - |
dc.contributor.AlternativeAuthor | 이윤일 | - |
dc.contributor.AlternativeAuthor | 서미란 | - |
dc.contributor.AlternativeAuthor | 김소영 | - |
dc.contributor.AlternativeAuthor | 이지은 | - |
dc.contributor.AlternativeAuthor | 윤홍덕 | - |
dc.contributor.AlternativeAuthor | 김용식 | - |
dc.contributor.AlternativeAuthor | 전용성 | - |
dc.identifier.doi | 10.1111/j.1471-4159.2009.06318.x | - |
dc.citation.journaltitle | JOURNAL OF NEUROCHEMISTRY | - |
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dc.description.tc | 9 | - |
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