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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Blotting, Western
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Bucladesine / pharmacology
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CREB-Binding Protein
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Calcium-Calmodulin-Dependent Protein Kinases / isolation & purification
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
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Enzyme Activation
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Mitogen-Activated Protein Kinase 1 / isolation & purification
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Mitogen-Activated Protein Kinase 1 / metabolism*
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Mitogen-Activated Protein Kinase 3
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Mitogen-Activated Protein Kinases*
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Nerve Growth Factors / pharmacology*
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Neurons / drug effects
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Neurons / physiology
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Nuclear Proteins / isolation & purification
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Nuclear Proteins / metabolism*
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PC12 Cells
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Phosphorylation
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Rats
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Signal Transduction / drug effects
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Signal Transduction / physiology
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Trans-Activators / isolation & purification
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Trans-Activators / metabolism*
Substances
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Nerve Growth Factors
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Nuclear Proteins
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Trans-Activators
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Bucladesine
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CREB-Binding Protein
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Crebbp protein, rat
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Calcium-Calmodulin-Dependent Protein Kinases
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Mitogen-Activated Protein Kinase 1
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Mitogen-Activated Protein Kinase 3
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Mitogen-Activated Protein Kinases