CBP: a signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV

S Chawla, G E Hardingham, D R Quinn, H Bading

Research output: Contribution to journalArticlepeer-review


Recruitment of the coactivator, CREB binding protein (CBP), by signal-regulated transcription factors, such as CREB [adenosine 3', 5'-monophosphate (cAMP) response element binding protein], is critical for stimulation of gene expression. The mouse pituitary cell line AtT20 was used to show that the CBP recruitment step (CREB phosphorylation on serine-133) can be uncoupled from CREB/CBP-activated transcription. CBP was found to contain a signal-regulated transcriptional activation domain that is controlled by nuclear calcium and calcium/calmodulin-dependent (CaM) protein kinase IV and by cAMP. Cytoplasmic calcium signals that stimulate the Ras mitogen-activated protein kinase signaling cascade or expression of the activated form of Ras provided the CBP recruitment signal but did not increase CBP activity and failed to activate CREB- and CBP-mediated transcription. These results identify CBP as a signal-regulated transcriptional coactivator and define a regulatory role for nuclear calcium and cAMP in CBP-dependent gene expression.
Original languageEnglish
Pages (from-to)1505-9
Number of pages5
Issue number5382
Publication statusPublished - 1998


  • Animals
  • CREB-Binding Protein
  • Calcium
  • Calcium Channels
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinase Type 4
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cell Line
  • Cell Nucleus
  • Cyclic AMP
  • Cyclic AMP Response Element-Binding Protein
  • Cytoplasm
  • Genes, Reporter
  • Mice
  • Models, Genetic
  • Nuclear Proteins
  • Phosphorylation
  • Phosphoserine
  • Recombinant Fusion Proteins
  • Signal Transduction
  • Trans-Activators
  • Transcription, Genetic
  • Transcriptional Activation
  • ras Proteins

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