ArticleAnnals of botany2016
Light-dependent activation of phosphoenolpyruvate carboxylase by reversible phosphorylation in cluster roots of white lupin plants: diurnal control in response to photosynthate supply.
Article in Annals of botany, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Functional metatranscriptomics of the rhizosphere: towards an understanding of metabolic processes of the microbial carbon pump.FEMS microbiology ecology · 2026Article
- The sucrose-trehalose 6-phosphate nexus is conserved in flowering plants with different phloem loading and carbon storage strategies.Journal of experimental botany · 2026Article
- Effect of variable phosphorus availability on root mechanisms involved in mobilization of the soil P in three lupine species.Scientific reports · 2025Article
- The white lupin trehalase gene LaTRE1 regulates cluster root formation and function under phosphorus deficiency.Plant physiology · 2024Article
- Metabolic footprints in phosphate-starved plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023Review
- Potential metabolic mechanisms for inhibited chloroplast nitrogen assimilation under high CO2.Plant physiology · 2021Article
- Leaf Phosphorus Concentration Regulates the Development of Cluster Roots and Exudation of Carboxylates inFrontiers in plant science · 2020Article
- A Tale of Two Sugars: Trehalose 6-Phosphate and Sucrose.Plant physiology · 2016Review
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Authors and funding
4 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background and Aims Phosphoenolpyruvate carboxylase (PEPC) is a tightly regulated enzyme that controls carbohydrate partitioning to organic acid anions (malate, citrate) excreted in copious amounts by cluster roots of inorganic phosphate (Pi)-deprived white lupin plants. Excreted malate and citrate solubilize otherwise inaccessible sources of mineralized soil Pi for plant uptake. The aim of this study was to test the hypotheses that (1) PEPC is post-translationally activated by reversible phosphorylation in cluster roots of illuminated white lupin plants, and (2) light-dependent phosphorylation of cluster root PEPC is associated with elevated intracellular levels of sucrose and its signalling metabolite, trehalose-6-phosphate. Methods White lupin plants were cultivated hydroponically at low Pi levels (≤1 µm) and subjected to various light/dark pretreatments. Cluster root PEPC activity and in vivo phosphorylation status were analysed to assess the enzyme's diurnal, post-translational control in response to light and dark. Levels of various metabolites, including sucrose and trehalose-6-phosphate, were also quantified in cluster root extracts using enzymatic and spectrometric methods. Key Results During the daytime the cluster root PEPC was activated by phosphorylation at its conserved N-terminal seryl residue. Darkness triggered a progressive reduction in PEPC phosphorylation to undetectable levels, and this was correlated with 75-80 % decreases in concentrations of sucrose and trehalose-6- phosphate. Conclusions Reversible, light-dependent regulatory PEPC phosphorylation occurs in cluster roots of Pi-deprived white lupin plants. This likely facilitates the well-documented light- and sucrose-dependent exudation of Pi-solubilizing organic acid anions by the cluster roots. PEPC's in vivo phosphorylation status appears to be modulated by sucrose translocated from CO2-fixing leaves into the non-photosynthetic cluster roots.
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