ReviewFrontiers in plant science2013
Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties.
Review in Frontiers in plant science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
93 citing papers in PubMed, 186 citations in OpenAlex.
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- Identification of the Glyceraldehyde-3-Phosphate Dehydrogenase (Plants (Basel, Switzerland) · 2025Article
- Beyond glycolysis: multifunctional roles of glyceraldehyde-3-phosphate dehydrogenases in plants.Horticulture research · 2025Article
- Cytosolic glyceraldehyde-3-phosphate dehydrogenase regulates plant stem cell maintenance under oxidative stress.Plant cell reports · 2025Article
- Regulation of plant glycolysis and the tricarboxylic acid cycle by posttranslational modifications.The Plant journal : for cell and molecular biology · 2025Review
- Exploration of key genes and pathways in response to submergence stress in red clover (Trifolium pratense L.) by WGCNA.BMC plant biology · 2025Article
- The regulatory impact of serine/threonine-specific protein phosphorylation among cyanobacteria.Frontiers in plant science · 2025Review
- Perception and processing of stress signals by plant mitochondria.The Plant journal : for cell and molecular biology · 2024Review
- Characterization of a Small Cysteine-Rich Secreted Effector, TcSCP_9014, inPlants (Basel, Switzerland) · 2024Article
- Genetic evidence for functions of Chloroplast CA in Pyropia yezoensis: decreased CCM but increased starch accumulation.Advanced biotechnology · 2024Article
- Evaluation of Cellular Responses byMicroorganisms · 2024Article
- Chloroplasts lacking class I glutaredoxins are functional but show a delayed recovery of protein cysteinyl redox state after oxidative challenge.Redox biology · 2024Article
- TheFrontiers in plant science · 2024Article
- Identification and expression profiling ofFrontiers in plant science · 2024Article
33 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme involved in glycolysis and shown, particularly in animal cells, to play additional roles in several unrelated non-metabolic processes such as control of gene expression and apoptosis. This functional versatility is regulated, in part at least, by redox post-translational modifications that alter GAPDH catalytic activity and influence the subcellular localization of the enzyme. In spite of the well established moonlighting (multifunctional) properties of animal GAPDH, little is known about non-metabolic roles of GAPDH in plants. Plant cells contain several GAPDH isoforms with different catalytic and regulatory properties, located both in the cytoplasm and in plastids, and participating in glycolysis and the Calvin-Benson cycle. A general feature of all GAPDH proteins is the presence of an acidic catalytic cysteine in the active site that is overly sensitive to oxidative modifications, including glutathionylation and S-nitrosylation. In Arabidopsis, oxidatively modified cytoplasmic GAPDH has been successfully used as a tool to investigate the role of reduced glutathione, thioredoxins and glutaredoxins in the control of different types of redox post-translational modifications. Oxidative modifications inhibit GAPDH activity, but might enable additional functions in plant cells. Mounting evidence support the concept that plant cytoplasmic GAPDH may fulfill alternative, non-metabolic functions that are triggered by redox post-translational modifications of the protein under stress conditions. The aim of this review is to detail the molecular mechanisms underlying the redox regulation of plant cytoplasmic GAPDH in the light of its crystal structure, and to provide a brief inventory of the well known redox-dependent multi-facetted properties of animal GAPDH, together with the emerging roles of oxidatively modified GAPDH in stress signaling pathways in plants.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.