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FEBS Lett. 1994 Jun 27;347(2-3):128-32.

14-3-3 proteins bind to histone and affect both histone phosphorylation and dephosphorylation.

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Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.


14-3-3 proteins appear to play a critical role in Ca(2+)-stimulated secretion in permeabilized chromaffin cells. 14-3-3 proteins have been reported to be both stimulators and inhibitors of protein kinase C (PKC). We have found that 14-3-3 proteins, isolated on the basis of their ability to enhance secretory activity, stimulated histone phosphorylation by PKC, but they had no effect on myosin light chain phosphorylation by PKC. 14-3-3 proteins were also found to inhibit the rate of [32P]histone dephosphorylation but not the rate of [32P]myosin light chain dephosphorylation. Cross-linking experiments and affinity chromatography demonstrated that 14-3-3 proteins bind to histones. These results suggest that at least some of the reported effects of 14-3-3 proteins on PKC activity may result from 14-3-3 proteins binding to histone.

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