Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1999-7-22
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0959-4965
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1239-43
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10363932-Animals, pubmed-meshheading:10363932-Blotting, Western, pubmed-meshheading:10363932-Bucladesine, pubmed-meshheading:10363932-CREB-Binding Protein, pubmed-meshheading:10363932-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:10363932-Enzyme Activation, pubmed-meshheading:10363932-Mitogen-Activated Protein Kinase 1, pubmed-meshheading:10363932-Mitogen-Activated Protein Kinase 3, pubmed-meshheading:10363932-Mitogen-Activated Protein Kinases, pubmed-meshheading:10363932-Nerve Growth Factors, pubmed-meshheading:10363932-Neurons, pubmed-meshheading:10363932-Nuclear Proteins, pubmed-meshheading:10363932-PC12 Cells, pubmed-meshheading:10363932-Phosphorylation, pubmed-meshheading:10363932-Rats, pubmed-meshheading:10363932-Signal Transduction, pubmed-meshheading:10363932-Trans-Activators
pubmed:year
1999
pubmed:articleTitle
CBP associates with the p42/p44 MAPK enzymes and is phosphorylated following NGF treatment.
pubmed:affiliation
Department of Molecular Pathology, Windeyer Institute of Medical Sciences, University College London, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't