ArticleJournal of experimental botany2014
In vivo monoubiquitination of anaplerotic phosphoenolpyruvate carboxylase occurs at Lys624 in germinating sorghum seeds.
Article in Journal of experimental botany, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 35 citations in OpenAlex.
- Unravelling the Significance of Phosphoenolpyruvate Carboxylase in Phosphate Starvation Responses.Plant, cell & environment · 2026Article
- Regulation of plant glycolysis and the tricarboxylic acid cycle by posttranslational modifications.The Plant journal : for cell and molecular biology · 2025Review
- Silencing of SbPlants (Basel, Switzerland) · 2023Article
- An In vitro Assay to Recapitulate Hormone-Triggered and SCF-Mediated Protein Ubiquitylation.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Comparative Ubiquitination Proteomics Revealed the Salt Tolerance Mechanism in Sugar Beet Monomeric Additional Line M14.International journal of molecular sciences · 2022Article
- Knock-down of phosphoenolpyruvate carboxylase 3 negatively impacts growth, productivity, and responses to salt stress in sorghum (Sorghum bicolor L.).The Plant journal : for cell and molecular biology · 2022Article
- Differential Expression, Tissue-Specific Distribution, and Posttranslational Controls of Phosphoenolpyruvate Carboxylase.Plants (Basel, Switzerland) · 2021Review
- Article
- Genetic and Pharmacological Inhibition of Autophagy increases the Monoubiquitination of Non-Photosynthetic PhosphoPlants (Basel, Switzerland) · 2020Article
- Large-scale Identification and Time-course Quantification of Ubiquitylation Events During Maize Seedling De-etiolation.Genomics, proteomics & bioinformatics · 2019Article
- Anionic Phospholipids Induce Conformational Changes in Phosphoenolpyruvate Carboxylase to Increase Sensitivity to Cathepsin Proteases.Frontiers in plant science · 2019Article
- Transport and Use of Bicarbonate in Plants: Current Knowledge and Challenges Ahead.International journal of molecular sciences · 2018Review
- Transcript profiling indicates a widespread role for bacterial-type phosphoenolpyruvate carboxylase in malate-accumulating sink tissues.Journal of experimental botany · 2017Article
- Article
- Regulatory Phosphorylation of Bacterial-Type PEP Carboxylase by the CaPlant physiology · 2017Article
- Article
- Light-dependent activation of phosphoenolpyruvate carboxylase by reversible phosphorylation in cluster roots of white lupin plants: diurnal control in response to photosynthate supply.Annals of botany · 2016Article
- New insights into the post-translational modification of multiple phosphoenolpyruvate carboxylase isoenzymes by phosphorylation and monoubiquitination during sorghum seed development and germination.Journal of experimental botany · 2016Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) is an important cytosolic regulatory enzyme that plays a pivotal role in numerous physiological processes in plants, including seed development and germination. Previous studies demonstrated the occurrence of immunoreactive PEPC polypeptides of ~110 kDa and 107 kDa (p110 and p107, respectively) on immunoblots of clarified extracts of germinating sorghum (Sorghum bicolor) seeds. In order to establish the biochemical basis for this observation, a 460 kDa PEPC heterotetramer composed of an equivalent ratio of p110 and p107 subunits was purified to near homogeneity from the germinated seeds. Mass spectrometry established that p110 and p107 are both encoded by the same plant-type PEPC gene (CP21), but that p107 was in vivo monoubiquitinated at Lys624 to form p110. This residue is absolutely conserved in vascular plant PEPCs and is proximal to a PEP-binding/catalytic domain. Anti-ubiquitin IgG immunodetected p110 but not p107, whereas incubation with a deubiquitinating enzyme (USP-2 core) efficiently converted p110 into p107, while relieving the enzyme's feedback inhibition by L-malate. Partial PEPC monoubiquitination was also detected during sorghum seed development. It is apparent that monoubiquitination at Lys624 is opposed to phosphorylation at Ser7 in terms of regulating the catalytic activity of sorghum seed PEPC. PEPC monoubiquitination is hypothesized to fine-tune anaplerotic carbon flux according to the cell's immediate physiological requirements for tricarboxylic acid cycle intermediates needed in support of biosynthesis and carbon-nitrogen interactions.
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