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. 2015 Nov;169(3):1469-87.
doi: 10.1104/pp.15.01378. Epub 2015 Sep 3.

Posttranslational Protein Modifications in Plant Metabolism

Affiliations

Posttranslational Protein Modifications in Plant Metabolism

Giulia Friso et al. Plant Physiol. 2015 Nov.

Abstract

Posttranslational modifications (PTMs) of proteins greatly expand proteome diversity, increase functionality, and allow for rapid responses, all at relatively low costs for the cell. PTMs play key roles in plants through their impact on signaling, gene expression, protein stability and interactions, and enzyme kinetics. Following a brief discussion of the experimental and bioinformatics challenges of PTM identification, localization, and quantification (occupancy), a concise overview is provided of the major PTMs and their (potential) functional consequences in plants, with emphasis on plant metabolism. Classic examples that illustrate the regulation of plant metabolic enzymes and pathways by PTMs and their cross talk are summarized. Recent large-scale proteomics studies mapped many PTMs to a wide range of metabolic functions. Unraveling of the PTM code, i.e. a predictive understanding of the (combinatorial) consequences of PTMs, is needed to convert this growing wealth of data into an understanding of plant metabolic regulation.

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Figures

Figure 1.
Figure 1.
Examples of PTMs regulating metabolic enzymes and pathways. A, Regulation of cytosolic phosphoenolpyruvate carboxylase (PEPC) in C4 plants such as maize. The regulation of PEPC kinases and phosphatase is still unknown, but it may involve additional PTMs. The cellular concentration of PEPC kinase is kept very low through proteasomal degradation. PEP, Phosphoenolpyruvate. B, Regulation of mitochondrial pyruvate dehydrogenase (PDH) by (de)phosphorylation through a PDH kinase and phosphatase. The PDH kinase is allosterically inhibited by pyruvate and stimulated by ammonia (produced through photorespiration), ensuring cross talk between PDH activity and the cellular metabolic state. C, Regulation of heterotetrameric ADP-Glc pyrophosphorylase (AGPase) by NADP-dependent thioredoxin reductase (NTRC) and thioredoxin. AGPase has two large and two small subunits; thioredoxin can reduce the disulfide bond (S-S) between the two small subunits, resulting in activation of the enzyme. In this activated state, AGPase is allosterically inhibited by inorganic phosphate (Pi) and stimulated by 3-phosphoglyceraldehyde (3-PGA), ensuring cross-talk between AGPase activity and the cellular metabolic state. D, Sequential PTMs control the adaptive response of plants to hypoxia through enzymatic oxygen-dependent Cys PTMs (sulfinic acid and sulfonic acid) of the transcriptional factor ERF-VII. Nitric oxide (NO) can also contribute to the Cys oxidation. The modified Cys is the N terminus of ERF-VII. RC, Arg-Cys.

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