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Updated: Oct 20, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP
Published on: May 26, 2017
CBP associates with the p42/p44 MAPK enzymes and is phosphorylated following NGF treatment
Y Z Liu1, N S Thomas, D S Latchman
1Department of Molecular Pathology, Windeyer Institute of Medical Sciences, University College London, UK.
Abstract:
The ability of the CBP (CREB binding protein) coactivator to stimulate transcription has previously been shown to be stimulated by treatment of neuronal cells with nerve growth factor (NGF). This effect is dependent upon activation of the p42/p44 MAPK (mitogen activated protein kinase) pathway. Here we show that both CBP and the related p300 protein directly associate with the p42/p44 MAPK enzymes both prior to and following their activation by NGF and that CBP is phosphorylated following NGF treatment. These results indicate that phosphorylation of CBP itself by the p42/p44 MAPK pathway is likely to be critical for its role in NGF-mediated stimulation of gene expression.
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