14-3-3-PROTEINS BIND TO HISTONE AND AFFECT BOTH HISTONE PHOSPHORYLATION AND DEPHOSPHORYLATION

被引：32
作者：
CHEN, FS
WAGNER, PD
机构：
[1] Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda
来源：
FEBS LETTERS | 1994年 / 347卷 / 2-3期
关键词：
14-3-3; PROTEIN; PROTEIN PHOSPHATASE; PROTEIN KINASE C; SECRETION;
D O I：
10.1016/0014-5793(94)00520-6
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
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 [P-32]histone dephosphorylation but not the rate of [P-32]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.
引用
收藏
页码：128 / 132
页数：5
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