In vivo regulation of glycogen synthase kinase 3β activity in neurons and brains

Abstract Glycogen synthase kinase 3β (GSK3β) is a multifunctional protein kinase involved in many cellular activities including development, differentiation and diseases. GSK3β is thought to be constitutively activated by autophosphorylation at Tyr216 and inactivated by phosphorylation at Ser9. The...

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Autores principales:	Ambika Krishnankutty, Taeko Kimura, Taro Saito, Kyota Aoyagi, Akiko Asada, Shin-Ichiro Takahashi, Kanae Ando, Mica Ohara-Imaizumi, Koichi Ishiguro, Shin-ichi Hisanaga
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/68c8c3b988af4b71b0daec8587131529
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spelling	oai:doaj.org-article:68c8c3b988af4b71b0daec85871315292021-12-02T15:05:39ZIn vivo regulation of glycogen synthase kinase 3β activity in neurons and brains10.1038/s41598-017-09239-52045-2322https://doaj.org/article/68c8c3b988af4b71b0daec85871315292017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-09239-5https://doaj.org/toc/2045-2322Abstract Glycogen synthase kinase 3β (GSK3β) is a multifunctional protein kinase involved in many cellular activities including development, differentiation and diseases. GSK3β is thought to be constitutively activated by autophosphorylation at Tyr216 and inactivated by phosphorylation at Ser9. The GSK3β activity has previously been evaluated by inhibitory Ser9 phosphorylation, but it does not necessarily indicate the kinase activity itself. Here, we applied the Phos-tag SDS-PAGE technique to the analysis of GSK3β phosphoisotypes in cells and brains. There were three phosphoisotypes of GSK3β; double phosphorylation at Ser9 and Tyr216, single phosphorylation at Tyr216 and the nonphosphorylated isotype. Active GSK3β with phosphorylation at Tyr216 represented half or more of the total GSK3β in cultured cells. Although levels of phospho-Ser9 were increased by insulin treatment, Ser9 phosphorylation occurred only in a minor fraction of GSK3β. In mouse brains, GSK3β was principally in the active form with little Ser9 phosphorylation, and the phosphoisotypes of GSK3β changed depending on the regions of the brain, age, sex and disease conditions. These results indicate that the Phos-tag SDS-PAGE method provides a simple and appropriate measurement of active GSK3β in vivo, and the activity is regulated by the mechanism other than phosphorylation on Ser9.Ambika KrishnankuttyTaeko KimuraTaro SaitoKyota AoyagiAkiko AsadaShin-Ichiro TakahashiKanae AndoMica Ohara-ImaizumiKoichi IshiguroShin-ichi HisanagaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-15 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ambika Krishnankutty Taeko Kimura Taro Saito Kyota Aoyagi Akiko Asada Shin-Ichiro Takahashi Kanae Ando Mica Ohara-Imaizumi Koichi Ishiguro Shin-ichi Hisanaga In vivo regulation of glycogen synthase kinase 3β activity in neurons and brains
description	Abstract Glycogen synthase kinase 3β (GSK3β) is a multifunctional protein kinase involved in many cellular activities including development, differentiation and diseases. GSK3β is thought to be constitutively activated by autophosphorylation at Tyr216 and inactivated by phosphorylation at Ser9. The GSK3β activity has previously been evaluated by inhibitory Ser9 phosphorylation, but it does not necessarily indicate the kinase activity itself. Here, we applied the Phos-tag SDS-PAGE technique to the analysis of GSK3β phosphoisotypes in cells and brains. There were three phosphoisotypes of GSK3β; double phosphorylation at Ser9 and Tyr216, single phosphorylation at Tyr216 and the nonphosphorylated isotype. Active GSK3β with phosphorylation at Tyr216 represented half or more of the total GSK3β in cultured cells. Although levels of phospho-Ser9 were increased by insulin treatment, Ser9 phosphorylation occurred only in a minor fraction of GSK3β. In mouse brains, GSK3β was principally in the active form with little Ser9 phosphorylation, and the phosphoisotypes of GSK3β changed depending on the regions of the brain, age, sex and disease conditions. These results indicate that the Phos-tag SDS-PAGE method provides a simple and appropriate measurement of active GSK3β in vivo, and the activity is regulated by the mechanism other than phosphorylation on Ser9.
format	article
author	Ambika Krishnankutty Taeko Kimura Taro Saito Kyota Aoyagi Akiko Asada Shin-Ichiro Takahashi Kanae Ando Mica Ohara-Imaizumi Koichi Ishiguro Shin-ichi Hisanaga
author_facet	Ambika Krishnankutty Taeko Kimura Taro Saito Kyota Aoyagi Akiko Asada Shin-Ichiro Takahashi Kanae Ando Mica Ohara-Imaizumi Koichi Ishiguro Shin-ichi Hisanaga
author_sort	Ambika Krishnankutty
title	In vivo regulation of glycogen synthase kinase 3β activity in neurons and brains
title_short	In vivo regulation of glycogen synthase kinase 3β activity in neurons and brains
title_full	In vivo regulation of glycogen synthase kinase 3β activity in neurons and brains
title_fullStr	In vivo regulation of glycogen synthase kinase 3β activity in neurons and brains
title_full_unstemmed	In vivo regulation of glycogen synthase kinase 3β activity in neurons and brains
title_sort	in vivo regulation of glycogen synthase kinase 3β activity in neurons and brains
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/68c8c3b988af4b71b0daec8587131529
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In vivo regulation of glycogen synthase kinase 3β activity in neurons and brains

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