Binding of a nuclear protein to the cyclic-AMP response element of the somatostatin gene

  title={Binding of a nuclear protein to the cyclic-AMP response element of the somatostatin gene},
  author={Marc Montminy and Louise M. Bilezikjian},
Many hormones act on neuroendocrine cells by activating second messenger pathways. Two of these, the phosphoinositol and cAMP-dependent pathways, cause changes in cellular activity through specific protein kinases. By phosphorylating cytoplasmic and nuclear proteins, these kinases apparently coordinate cellular processes, including the biosynthesis and release of neuropeptides. Somatostatin biosynthesis and release, for example, are both positively regulated by the second messenger cAMP in… Expand
Regulation of somatostatin gene transcription by cAMP.
CAMP functions as a starvation state signal, mediating hormonal cues from the pancreas and adrenal gland to stimulate glucose production and regulating transcription of the gene for phosphoenolpyruvate carboxykinase (PEPCK), a rate-limiting enzyme in gluconeogenesis. Expand
Regulation of somatostatin gene transcription by cyclic adenosine monophosphate.
An antiserum directed against amino acid 634-648 within the CREB-binding domain of CBP, which specifically recognizes sequences within the Ser133 phosphorylated form of CREB, critical for PK-A-inducible transcription. Expand
Regulation of somatostatin gene transcription by cAMP.
Testing whether CREB activity in response to cAMP might be dependent on phosphorylation by PKA found that mutant cell lines deficient in PKA cannot support CAMP- responsive transcription from a CRE reporter gene, suggesting that this kinase might phosphorylate proteins that bind to the CRE and, thereby activate transcription of cAMP-responsive genes. Expand
Cyclic AMP response element-binding protein and the catalytic subunit of protein kinase A are present in F9 embryonal carcinoma cells but are unable to activate the somatostatin promoter
The cyclic AMP (cAMP) response elements (CREs) of the somatostatin and vasoactive intestinal peptide (VIP) promoters contain binding sites for CRE-binding protein (CREB) that are essential forExpand
A common trans-acting factor is involved in transcriptional regulation of neurotransmitter genes by cyclic AMP
Activation of neurotransmitter receptors can regulate transcription in postsynaptic cells through the actions of second messengers. Trans-synaptic regulation of transcription appears to be anExpand
The cAMP response element binding protein is expressed and phosphorylated in cardiac myocytes.
Elevation of cAMP leads to phosphorylation of CREB-P and an increase in creb mRNA abundance, which is independent of the contractile state. Expand
Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine 133
Results suggest that phosphorylation of CREB may stimulate transcription by a mechanism other than by simply providing negative charge, as CREB mutants containing acidic residues in place of the Ser-133 phosphoacceptor were also transcriptionally inactive. Expand
A cluster of phosphorylation sites on the cyclic AMP-regulated nuclear factor CREB predicted by its sequence
The isolation of a cDNA clone for rat CREB is reported using amino-acid sequence information from purified CREB protein, which predicts a cluster ofprotein kinase A, protein kinase C and casein kinase II consensus recognition sites near the N terminus of the protein that may interact either positively or negatively to regulate CREB bioactivity. Expand
Synergistic activation of cAMP and calcium on cAMP-response-element-mediated gene expression in GH3 pituitary tumor cells.
Results indicate that cAMP and Ca2+ synergistically activated CRE-driven gene expression through non-overlapping phosphorylation events in GH3 cells is inhibited by the L-type Ca(2+)-channel blocker verapamil. Expand
cAMP-dependent regulation of gene transcription by cAMP response element-binding protein and cAMP response element modulator.
This chapter discusses cyclic AMP (cAMP)-dependent regulation of gene transcription by cAMP response element-binding protein and cAMPresponse element modulator, and the interplay between the phosphorylating protein kinases and the dephosphorylates protein phosphatases is critical in determining the relative transactivation potential at any given moment. Expand