CBP or CREB-binding protein is a nuclear transcriptional coactivator protein that binds specifically to the PKA-phosphorylated form of the CREB protein. Microinjection of an anti-CBP antiserum into fibroblasts leads to inhibition of transcription from a cAMP promoter. CBP can also cooperates with upstream activators, such as JUN. When JUN is phosphorylated at the transcriptionally stimulatory sites ser73 and ser63, it binds CBP with comparable affinity to CREB. Insulin signaling may directly regulate many cAMP signaling pathways at the transcriptional level by controlling CBP recruitment. Mutant CBP can be aberrantly recruited to CREB protein, resulting in inappropriate activation of gluconeogenesis and glucose intolerance.
Homodimers of the NF-kappa B p50 subunit are transcriptionally repressive in cells, whereas they can promote transcription in vitro, suggesting that their endogenous effects are mediated by association with other factors. We now demonstrate that transcriptionally inactive nuclear NF-kappaB in
A number of signalling pathways stimulate transcription of target genes through nuclear factors whose activities are primarily regulated by phosphorylation. Cyclic AMP regulates the expression of numerous genes, for example, through the protein kinase-A (PKA)-mediated phosphorylation of transcription factor CREB
Questions
Reviews
★★★★★ No rating value
Active Filters
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.