Function and specificity of 14-3-3 proteins in the regulation of carbohydrate and nitrogen metabolism.
Protein phosphorylation is key to the regulation of many proteins. Altered protein activity often requires the interaction of the phosphorylated protein with a class of "adapters" known as 14-3-3 proteins. This review will cover aspects of 14-3-3 interaction with key proteins of carbon and nitrogen metabolism such as nitrate reductase, glutamine synthetase and sucrose-phosphate synthase. It will also address 14-3-3 involvement in signal transduction pathways with emphasis on the regulation of plant metabolism. To date, 14-3-3 proteins have been identified and studied in many diverse systems, yielding a plethora of data, requiring careful analysis and interpretation. Problems such as these are not uncommon when dealing with multigene families. The number of isoforms makes the question of redundancy versus specificity of 14-3-3 proteins a crucial one. This issue is discussed in relation to structure, function and expression of 14-3-3 proteins.
Comparot
Sylviane
S
University of Cambridge, Department of Plant Sciences, Downing Site, Cambridge CB2 3EA, UK.
Lingiah
Gavin
G
Martin
Thomas
T
D048948:14-3-3 Proteins; D050260:Carbohydrate Metabolism; D018506:Gene Expression Regulation, Plant; D007473:Ion Channels / Q000378:metabolism; D009584:Nitrogen / Q000378:metabolism*; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology; D013379:Substrate Specificity; D014157:Transcription Factors / Q000378:metabolism; D014446:Tyrosine 3-Monooxygenase / Q000235:genetics / Q000378:metabolism*
D048948:14-3-3 Proteins; D007473:Ion Channels; D010940:Plant Proteins; D014157:Transcription Factors; D014446:Tyrosine 3-Monooxygenase; D006180:Proton-Translocating ATPases; D009584:Nitrogen