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Regulation of cytosolic enzymes in primary metabolism by reversible protein phosphorylation
1MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, DD1 4HN, Scotland, UK. cmackintosh@bad.dundee.ac.uk
Abstract:
Recent discoveries have revealed that cytosolic enzymes of sugar, amino acid, and isoprenoid synthesis, sucrose breakdown and the plasma membrane H+-ATPase are regulated by reversible protein (serine/threonine) phosphorylation. In some cases, phosphorylation creates a phosphopeptide motif that is recognized by and binds to 14-3-3 proteins, and 14-3-3 binding changes the activity of the enzyme or ion pump. Intriguing new clues hint at how these cytosolic regulatory networks might link to signalling pathways triggered by hormones, nutrients, stresses, circadian rhythms, and other factors that regulate the growth and development of the whole plant.