Calcium-Regulated Phosphorylation Within the Leucine Zipper of C/EBPβ

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Science  17 Apr 1992:
Vol. 256, Issue 5055, pp. 370-373
DOI: 10.1126/science.256.5055.370


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/EBPβ, a member of the bZip family of transcription factors. In pituitary cells C/EBPβ 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/EBPβ appeared to confer calcium-regulated transcriptional stimulation of a promoter that contained binding sites for C/EBPβ.

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