Glycogen synthase kinase-3β is tyrosine-phosphorylated by MEK1 in human skin fibroblasts

Fumi Takahashi-Yanaga, Fumie Shiraishi, Masato Hirata, Yoshikazu Miwa, Sachio Morimoto, Toshiyuki Sasaguri

研究成果: ジャーナルへの寄稿記事

37 引用 (Scopus)

抄録

Glycogen synthase kinase-3β (GSK-3β) can be associated with several proteins in cell. We analyzed the immunoprecipitates by an anti-GSK-3β antibody from cell lysate of human fibroblasts and found that this protein was co-precipitated with mitogen-activated protein kinase kinase (MEK1/2). U0126, a MEK1/2 inhibitor, inhibited tyrosine phosphorylation of GSK-3β, suggesting that MEK1/2 was involved in the phosphorylation of Tyr216 in GSK-3β. In vitro kinase assay was carried out using a recombinant human active MEK1 and we found that GSK-3β was phosphorylated on Tyr216 by this kinase in a dose- and time-dependent manner. Further, the pretreatment of fibroblasts with U0126 inhibited serum-induced nuclear translocation of GSK-3β. These results suggested that MEK1/2 induces tyrosine phosphorylation of GSK-3β and this cellular event might induce nuclear translocation of GSK-3β. This is the first report to suggest that MEK1/2 phosphorylates not only ERK1/2 but also GSK-3β.

元の言語英語
ページ(範囲)411-415
ページ数5
ジャーナルBiochemical and Biophysical Research Communications
316
発行部数2
DOI
出版物ステータス出版済み - 4 2 2004

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Glycogen Synthase Kinase 3
Fibroblasts
Tyrosine
Skin
Phosphorylation
Phosphotransferases
MAP Kinase Kinase 2
3-tyrosine
Mitogen-Activated Protein Kinase Kinases
Assays
Proteins

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Glycogen synthase kinase-3β is tyrosine-phosphorylated by MEK1 in human skin fibroblasts. / Takahashi-Yanaga, Fumi; Shiraishi, Fumie; Hirata, Masato; Miwa, Yoshikazu; Morimoto, Sachio; Sasaguri, Toshiyuki.

:: Biochemical and Biophysical Research Communications, 巻 316, 番号 2, 02.04.2004, p. 411-415.

研究成果: ジャーナルへの寄稿記事

Takahashi-Yanaga, Fumi ; Shiraishi, Fumie ; Hirata, Masato ; Miwa, Yoshikazu ; Morimoto, Sachio ; Sasaguri, Toshiyuki. / Glycogen synthase kinase-3β is tyrosine-phosphorylated by MEK1 in human skin fibroblasts. :: Biochemical and Biophysical Research Communications. 2004 ; 巻 316, 番号 2. pp. 411-415.
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abstract = "Glycogen synthase kinase-3β (GSK-3β) can be associated with several proteins in cell. We analyzed the immunoprecipitates by an anti-GSK-3β antibody from cell lysate of human fibroblasts and found that this protein was co-precipitated with mitogen-activated protein kinase kinase (MEK1/2). U0126, a MEK1/2 inhibitor, inhibited tyrosine phosphorylation of GSK-3β, suggesting that MEK1/2 was involved in the phosphorylation of Tyr216 in GSK-3β. In vitro kinase assay was carried out using a recombinant human active MEK1 and we found that GSK-3β was phosphorylated on Tyr216 by this kinase in a dose- and time-dependent manner. Further, the pretreatment of fibroblasts with U0126 inhibited serum-induced nuclear translocation of GSK-3β. These results suggested that MEK1/2 induces tyrosine phosphorylation of GSK-3β and this cellular event might induce nuclear translocation of GSK-3β. This is the first report to suggest that MEK1/2 phosphorylates not only ERK1/2 but also GSK-3β.",
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AU - Miwa, Yoshikazu

AU - Morimoto, Sachio

AU - Sasaguri, Toshiyuki

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AB - Glycogen synthase kinase-3β (GSK-3β) can be associated with several proteins in cell. We analyzed the immunoprecipitates by an anti-GSK-3β antibody from cell lysate of human fibroblasts and found that this protein was co-precipitated with mitogen-activated protein kinase kinase (MEK1/2). U0126, a MEK1/2 inhibitor, inhibited tyrosine phosphorylation of GSK-3β, suggesting that MEK1/2 was involved in the phosphorylation of Tyr216 in GSK-3β. In vitro kinase assay was carried out using a recombinant human active MEK1 and we found that GSK-3β was phosphorylated on Tyr216 by this kinase in a dose- and time-dependent manner. Further, the pretreatment of fibroblasts with U0126 inhibited serum-induced nuclear translocation of GSK-3β. These results suggested that MEK1/2 induces tyrosine phosphorylation of GSK-3β and this cellular event might induce nuclear translocation of GSK-3β. This is the first report to suggest that MEK1/2 phosphorylates not only ERK1/2 but also GSK-3β.

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