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. 2000 Feb 21;148(4):691–702. doi: 10.1083/jcb.148.4.691

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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GBP does not inhibit Xgsk-3 phosphorylation of a peptide substrate. Embryos were injected with RNA encoding Xgsk-3-myc together with control RNA or GBP-FLAG RNA. After 3 h, proteins were extracted and immunoprecipitated with anti-FLAG (Xgsk-3 + GBP), anti-myc (Xgsk-3 + control), or both (uninjected) antibodies. The kinase activity of immune complexes was measured by phosphorus-32 incorporation into the GSK-3–specific substrate prephosphorylated CREB peptide (p-CREB; dark bars). The nonphosphorylated CREB peptide (CREB; light bars) is not a GSK-3 substrate and was used as a control. The activity of duplicate immune complexes is shown.