14‐3‐3 proteins bind to histone and affect both histone phosphorylation and dephosphorylation

FEBS Letters

Chen, Fusheng¹  Wagner, Paul D.¹ 

[1] Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA

关键词: 14-3-3 protein;    Protein phosphatase;    Protein kinase C;    Secretion;    EGTA;    [ethylenebis(oxyethylenenitrilo)] tetraacetic acid;    HEPES;    4-(2-hydroxyethyl)-1-piperazineethane sulfonic acid;    KCIPs;    kinase C inhibitor proteins;    PKC;    protein kinase C;    PP1;    protein phosphatase 1;    PP2A;    protein phosphatase 2A;   

DOI  :  10.1016/0014-5793(94)00520-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

14-3-3 proteins appear to play a critical role in Ca²⁺-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.

【 授权许可】

Unknown