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Calcium-dependent phosphorylation of histone H3 in butyrate-treated HeLa cells

Nature volume 287, pages 74–76 (1980)Cite this article

Abstract

Ca2+ is prominant in the control of cell proliferation and function1,2. However, the biochemical mechanism(s) mediating its effects on nuclear events is unknown. We report here that Ca2+, at physiological concentrations, stimulates the phosphorylation of histone H3 by an endogenous protein kinase in HeLa cell nuclei. Also, pretreatment of cells with Na butyrate, which increases histone acetylation, selectively increases the susceptibility of histone H3 to phosphorylation by the protein kinase. Our results reveal a potential link between histone H3 acetylation and phosphorylation, modifications which are thought to have important effects on chromatin structure and function and suggest a possible mechanism whereby stimuli at the cell surface (such as hormones, mitogens and drugs) may influence biochemical events at the nuclear level; changes in the intracellular Ca2+ concentration may influence the phosphorylation of chromosomal proteins, mediated by Ca2+-dependent kinases in the nucleus.

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Authors and Affiliations

  1. Department of Pharmacology, Stanford University School of Medicine, Stanford, California, 94305

    James P. Whitlock Jr, Robert Augustine & Howard Schulman

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  1. James P. Whitlock Jr
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  2. Robert Augustine
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  3. Howard Schulman
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Whitlock, J., Augustine, R. & Schulman, H. Calcium-dependent phosphorylation of histone H3 in butyrate-treated HeLa cells. Nature 287, 74–76 (1980). https://doi.org/10.1038/287074a0

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