Calcium-regulated phosphorylation within the leucine zipper of C/EBP beta

Science. 1992 Apr 17;256(5055):370-3. doi: 10.1126/science.256.5055.370.

Abstract

Alterations in intracellular calcium levels activate several signal transduction pathways resulting in distinct patterns of gene expression. Here, a pathway for calcium-mediated signals is demonstrated that involves C/EBP beta, a member of the bZip family of transcription factors. In pituitary cells C/EBP beta was phosphorylated in response to increased intracellular calcium concentrations as a consequence of the activation of a calcium-calmodulin-dependent protein kinase. Phosphorylation of serine at position 276 within the leucine zipper of C/EBP beta appeared to confer calcium-regulated transcriptional stimulation of a promoter that contained binding sites for C/EBP beta.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • CCAAT-Enhancer-Binding Proteins
  • Calcimycin / pharmacology
  • Calcium / pharmacology*
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cell Line
  • DNA / chemistry
  • DNA / genetics
  • DNA / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Enzyme Activation / drug effects
  • Leucine Zippers*
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / metabolism*
  • Phosphorylation
  • Phosphoserine / metabolism
  • Pituitary Gland / metabolism
  • Protein Kinases / metabolism
  • Signal Transduction / drug effects
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism*
  • Transcription, Genetic / drug effects
  • Transfection

Substances

  • CCAAT-Enhancer-Binding Proteins
  • DNA-Binding Proteins
  • Nuclear Proteins
  • Transcription Factors
  • Phosphoserine
  • Calcimycin
  • DNA
  • Protein Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Calcium