14-3-3 proteins bind to histone and affect both histone phosphorylation and dephosphorylation.
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.
Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.
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Chen
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Wagner
D048948:14-3-3 Proteins; D000255:Adenosine Triphosphate / Q000378:metabolism; D000313:Adrenal Medulla / Q000737:chemistry; D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002846:Chromatography, Affinity; D003432:Cross-Linking Reagents; D004120:Dimethyl Suberimidate; D006657:Histones / Q000378:metabolism*; D007700:Kinetics; D009218:Myosins / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000378:metabolism* / Q000494:pharmacology; D016716:PC12 Cells; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D014446:Tyrosine 3-Monooxygenase
D048948:14-3-3 Proteins; D003432:Cross-Linking Reagents; D006657:Histones; D009419:Nerve Tissue Proteins; D004120:Dimethyl Suberimidate; D000255:Adenosine Triphosphate; D014446:Tyrosine 3-Monooxygenase; D011493:Protein Kinase C; D009218:Myosins