Metabolic enzymes as targets for 14-3-3 proteins

被引:120
作者
Huber, SC [1 ]
MacKintosh, C
Kaiser, WM
机构
[1] N Carolina State Univ, USDA ARS, Raleigh, NC 27695 USA
[2] N Carolina State Univ, Dept Crop Sci, Raleigh, NC 27695 USA
[3] N Carolina State Univ, Dept Bot, Raleigh, NC 27695 USA
[4] Univ Dundee, Dept Biochem, MRC, Prot Phosphorylat Unit, Dundee DD1 4HN, Scotland
[5] Univ Wurzburg, Julius Von Sachs Inst Biowissensch, D-97082 Wurzburg, Germany
基金
英国医学研究理事会; 英国生物技术与生命科学研究理事会;
关键词
14-3-3-affinity chromatography; divalent cations; glutamine synthetase; NADH : nitrate reductase; polyamines; proteolytic degradation; sucrose-phosphate synthase;
D O I
10.1023/A:1021284002779
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
The 14-3-3 proteins are binding proteins that have been shown to interact with a wide array of enzymes involved in primary biosynthetic and energy metabolism in plants. In most cases, the significance of binding of the 14-3-3 protein is not known. However, most of the interactions are phosphorylation-dependent and most of the known binding partners are found in the cytosol, while some may also be localized to plastids and mitochondria. In this review, we examine the factors that may regulate the binding of 14-3-3s to their target proteins, and discuss their possible roles in the regulation of the activity and proteolytic degradation of enzymes involved in primary carbon and nitrogen metabolism.
引用
收藏
页码:1053 / 1063
页数:11
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