CBP associates with the p42/p44 MAPK enzymes and is phosphorylated following NGF treatment.

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.

[1]  D. Latchman,et al.  Nerve Growth Factor Up-regulates the Transcriptional Activity of CBP through Activation of the p42/p44MAPK Cascade* , 1998, The Journal of Biological Chemistry.

[2]  B. Ebert,et al.  Regulation of Transcription by Hypoxia Requires a Multiprotein Complex That Includes Hypoxia-Inducible Factor 1, an Adjacent Transcription Factor, and p300/CREB Binding Protein , 1998, Molecular and Cellular Biology.

[3]  R. Kitsis,et al.  Transcriptional Coactivator p300 Stimulates Cell Type-specific Gene Expression in Cardiac Myocytes* , 1997, The Journal of Biological Chemistry.

[4]  N. Shiama The p300/CBP family: integrating signals with transcription factors and chromatin. , 1997, Trends in cell biology.

[5]  A. Nordheim,et al.  MAP kinase-dependent transcriptional coactivation by Elk-1 and its cofactor CBP. , 1996, Biochemical and biophysical research communications.

[6]  E. Krebs,et al.  The MAPK signaling cascade , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[7]  D. Latchman,et al.  The Cyclic AMP Response Element in the Calcitonin/Calcitonin Gene-related Peptide Gene Promoter Is Necessary but Not Sufficient for Its Activation by Nerve Growth Factor (*) , 1995, The Journal of Biological Chemistry.

[8]  C. Marshall,et al.  Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation , 1995, Cell.

[9]  M. Greenberg,et al.  Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB , 1994, Cell.

[10]  Kim Carr Nobel rewards two laboratory revolutions , 1993, Nature.

[11]  L. Greene,et al.  Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. , 1976, Proceedings of the National Academy of Sciences of the United States of America.