ArticleBMC plant biology2018
Cytosolic GAPDH as a redox-dependent regulator of energy metabolism.
Article in BMC plant biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 95 citations in OpenAlex.
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- Evaluation of Salivary GAPDH as a Predictor Biomarker for Periodontitis.International journal of molecular sciences · 2025Article
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- Comparative Proteomic Analysis of Popcorn Genotypes Identifies Differentially Accumulated Proteins Associated with Resistance Pathways to Southern Leaf Blight Disease.Plants (Basel, Switzerland) · 2025Article
- PNPO-Mediated Oxidation of DVL3 Promotes Multiple Myeloma Malignancy and Osteoclastogenesis by Activating the Wnt/β-Catenin Pathway.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Reactive oxygen species-post translational modifications-central carbon metabolism regulatory loop: coordination of redox homeostasis and carbon flux allocation in plants under abiotic stress.Frontiers in plant science · 2025Review
- Perception and processing of stress signals by plant mitochondria.The Plant journal : for cell and molecular biology · 2024Review
- The Key Enzymes of Carbon Metabolism and the Glutathione Antioxidant System ProtectJournal of fungi (Basel, Switzerland) · 2024Article
- Identification and expression profiling ofFrontiers in plant science · 2024Article
- Phosphatidic acid signaling and function in nuclei.Progress in lipid research · 2024Review
- Comparative transcriptomic and weighted gene co-expression network analysis to identify the core genes in the cultivars ofPlant signaling & behavior · 2023Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
backgroundPlant cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (GapC) displays redox-dependent changes in its subcellular localizations and activity. Apart from its fundamental role in glycolysis, it also exhibits moonlighting properties. Since the exceptional redox-sensitivity of GapC has been suggested to play a crucial role in its various functions, we here studied its redox-dependent subcellular localization and the influence of the redox-state on GapC protein interactions.
resultsIn mesophyll protoplasts from Arabidopsis thaliana, colocalization of GapC with mitochondria was more pronounced under reducing conditions than upon oxidative stress. In accordance, reduced GapC showed an increased affinity to the mitochondrial voltage-dependent anion-selective channel (VDAC) compared to the oxidized one. On the other hand, nuclear localization of GapC was increased under oxidizing conditions. The essential role of the catalytic cysteine for nuclear translocation was shown by using the corresponding cysteine mutants. Furthermore, interaction of GapC with the thioredoxin Trx-h3 as a candidate to revert the redox-modifications, occurred in the nucleus of oxidized protoplasts. In a yeast complementation assay, we could demonstrate that the plant-specific non-phosphorylating glyceraldehyde 3-P dehydrogenase (GapN) can substitute for glucose 6-P dehydrogenase to generate NADPH for re-reduction of the Trx system and ROS defense.
conclusionsThe preferred association of reduced, glycolytically active GapC with VDAC suggests a substrate-channeling metabolon at the mitochondrial surface for efficient energy generation. Increased occurrence of oxidized GapC in the nucleus points to a function in signal transduction and gene expression. Furthermore, the interaction of GapC with Trx-h3 in the nucleus indicates reversal of the oxidative cysteine modification after re-establishment of cellular homeostasis. Both, energy metabolism and signal transfer for long-term adjustment and protection from redox-imbalances are mediated by the various functions of GapC. The molecular properties of GapC as a redox-switch are key to its multiple roles in orchestrating energy metabolism.
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