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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding Sites
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CCAAT-Enhancer-Binding Proteins
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Calcimycin / pharmacology
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Calcium / pharmacology*
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Calcium-Calmodulin-Dependent Protein Kinases
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Cell Line
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DNA / chemistry
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DNA / genetics
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DNA / metabolism
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / metabolism*
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Enzyme Activation / drug effects
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Leucine Zippers*
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Molecular Sequence Data
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Nuclear Proteins / chemistry
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Nuclear Proteins / metabolism*
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Phosphorylation
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Phosphoserine / metabolism
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Pituitary Gland / metabolism
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Protein Kinases / metabolism
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Signal Transduction / drug effects
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Transcription Factors / chemistry
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Transcription Factors / metabolism*
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Transcription, Genetic / drug effects
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Transfection
Substances
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CCAAT-Enhancer-Binding Proteins
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DNA-Binding Proteins
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Nuclear Proteins
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Transcription Factors
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Phosphoserine
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Calcimycin
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DNA
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Protein Kinases
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Calcium-Calmodulin-Dependent Protein Kinases
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Calcium