Metabolic Regulation of Glyceraldehyde-3-Phosphate Dehydrogenases in Plants

Glyceraldehyde-3-phosphate dehydrogenases (GAPDHs) serve as pivotal enzymes in both glycolysis and the Calvin–Benson cycle, integrating carbon flux and energy production in plant cells. Metabolic regulation of GAPDHs is largely mediated by redox-sensitive post-translational modifications of a catalytic cysteine, which modulate enzyme activity, subcellular localisation and protein–protein interactions. Under reducing conditions, cytosolic GAPDHs engage in substrate-channeling metabolons at the mitochondrial surface to optimise ATP and NADH generation. Oxidative signals trigger nuclear translocation of GAPDH isoforms, where they moonlight as regulators of gene expression and stress signalling. Plastidial and cytosolic isoforms exhibit distinct roles in photosynthetic and non-photosynthetic tissues, contributing to reactive oxygen species homeostasis and adaptation to abiotic stresses. Advances in understanding these regulatory mechanisms open avenues for engineering stress resilience and improving carbon assimilation efficiency in crops.

Research from Nature Portfolio

Recent studies have revealed that heat stress induces nuclear accumulation of cytosolic GAPDH in Arabidopsis, where it binds to a heat-responsive transcription factor to promote the expression of protective genes. Overexpression of the enzyme enhances seedling survival at elevated temperatures, whereas loss of GAPDH function diminishes heat tolerance and disrupts transcriptional activation. This work elucidates a molecular mechanism by which a classic glycolytic enzyme moonlights as a direct regulator of stress-inducible gene networks.

Metabolic Regulation of Glyceraldehyde-3-Phosphate Dehydrogenases in Plants publication trend

The graph below shows the total number of articles in metabolic regulation of glyceraldehyde-3-phosphate dehydrogenases in plants across all publications each year (not limited to Nature Index journals).

Technical terms

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH): A conserved enzyme that catalyses the oxidation of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate, linking glycolysis and the Calvin–Benson cycle.

Redox post-translational modification: A reversible alteration of a protein’s cysteine residue by oxidation or reduction, affecting catalytic activity and interaction with partners.

Moonlighting protein: A protein that performs multiple, mechanistically distinct functions beyond its primary enzymatic activity.

Substrate-channeling metabolon: A transient multi-enzyme assembly that directly transfers metabolic intermediates between enzymes to enhance pathway efficiency.

Abiotic stress: Non-living environmental factors—such as temperature extremes, salinity and drought—that challenge plant physiological and metabolic homeostasis.

References

1. Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties. Frontiers in Plant Science (2013).
2. Transfer of a Redox-Signal through the Cytosol by Redox-Dependent Microcompartmentation of Glycolytic Enzymes at Mitochondria and Actin Cytoskeleton. Frontiers in Plant Science (2013).
3. Cytosolic GAPDH as a redox-dependent regulator of energy metabolism. BMC Plant Biology (2018).
4. Nuclear moonlighting of cytosolic glyceraldehyde-3-phosphate dehydrogenase regulates Arabidopsis response to heat stress. Nature Communications (2020).
5. The Plastidial Glyceraldehyde-3-Phosphate Dehydrogenase Is Critical for Abiotic Stress Response in Wheat. International Journal of Molecular Sciences (2019).
6. Genome-wide identification and analysis of glyceraldehyde-3-phosphate dehydrogenase family reveals the role of GmGAPDH14 to improve salt tolerance in soybean (Glycine max L.). Frontiers in Plant Science (2023).