Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB.
A nuclear protein, CREB, has been isolated from rat brain and shown to stimulate transcription of the cyclic AMP-responsive gene somatostatin as a dimer. Biochemical analysis suggests that dimerization and transcriptional efficacy of CREB protein in vitro are regulated by phosphorylation. These findings demonstrate that cellular signals can modulate gene expression by regulating the covalent modification of pre-existing nuclear factors.
D000123:Acetyltransferases / Q000235:genetics; D000818:Animals; D001923:Brain Chemistry; D015500:Chloramphenicol O-Acetyltransferase; D002845:Chromatography; D000242:Cyclic AMP / Q000494:pharmacology*; D004247:DNA / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D012091:Repetitive Sequences, Nucleic Acid; D013004:Somatostatin / Q000235:genetics; D014158:Transcription, Genetic; D014162:Transfection; D014407:Tumor Cells, Cultured
D046911:Macromolecular Substances; D009687:Nuclear Proteins; D013004:Somatostatin; D004247:DNA; D000242:Cyclic AMP; D000123:Acetyltransferases; D015500:Chloramphenicol O-Acetyltransferase; D011494:Protein Kinases; D011493:Protein Kinase C