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• W1438033008 abstract "Research Article1 January 1986free access Activation of a ribosomal protein S6 protein kinase in Xenopus oocytes by insulin and insulin-receptor kinase. D. Stefanovic D. Stefanovic Search for more papers by this author E. Erikson E. Erikson Search for more papers by this author L.J. Pike L.J. Pike Search for more papers by this author J.L. Maller J.L. Maller Search for more papers by this author D. Stefanovic D. Stefanovic Search for more papers by this author E. Erikson E. Erikson Search for more papers by this author L.J. Pike L.J. Pike Search for more papers by this author J.L. Maller J.L. Maller Search for more papers by this author Author Information D. Stefanovic, E. Erikson, L.J. Pike and J.L. Maller The EMBO Journal (1986)5:157-160https://doi.org/10.1002/j.1460-2075.1986.tb04190.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Previous studies in this laboratory have shown that insulin treatment of Xenopus oocytes leads to an increase in phosphorylation of ribosomal protein S6. To investigate the mechanism of this increase, S6 kinase activity was measured in lysates of oocytes exposed to insulin. Insulin caused a rapid 4- to 6-fold increase in S6 kinase activity, which was maximal by 20 min and which could be reversed by removal of insulin prior to homogenization. Dose-response curves showed a detectable increase in specific activity at 1 nM insulin with a maximal effect at 100 nM. Treatment of oocytes with puromycin did not prevent this increase in S6 kinase activity, suggesting activation rather than synthesis of the enzyme. DEAE-Sephacel chromatography of extracts from insulin-treated oocytes revealed two peaks of S6 kinase activity, and the specific activity of the peak eluting at 300 nM NaCl was increased 3-fold in oocytes treated with insulin. The same peak of S6 kinase activity was increased 40% within 10 min in oocytes injected with highly purified insulin-receptor kinase. These results indicate that the insulin-dependent increase in S6 phosphorylation is due, at least in part, to activation of an S6 protein kinase, and this activation may result from the action of the insulin receptor at an intracellular location. Previous ArticleNext Article Volume 5Issue 11 January 1986In this issue RelatedDetailsLoading ..." @default.
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• W1438033008 date "1986-01-01" @default.
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• W1438033008 title "Activation of a ribosomal protein S6 protein kinase in Xenopus oocytes by insulin and insulin-receptor kinase." @default.
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• W1438033008 doi "https://doi.org/10.1002/j.1460-2075.1986.tb04190.x" @default.
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