ArticlePlanta2006
Phosphorylation and subsequent interaction with 14-3-3 proteins regulate plastid glutamine synthetase in Medicago truncatula.
Article in Planta, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 58 citations in OpenAlex.
- Glutamine synthetase GLN1;5 and ACT domain repeat ACR1 functionally interact at the seed level in Arabidopsis thaliana.Protoplasma · 2026Article
- Glycine-Induced Phosphorylation Plays a Pivotal Role in Energy Metabolism in Roots and Amino Acid Metabolism in Leaves of Tea Plant.Foods (Basel, Switzerland) · 2023Article
- Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme.eLife · 2021Article
- Role of protein phosphatases in the regulation of nitrogen nutrition in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021Review
- Article
- Cytosolic Glutamine Synthetase Gln1;2 Is the Main Isozyme Contributing to GS1 Activity and Can Be Up-Regulated to Relieve Ammonium Toxicity.Plant physiology · 2016Article
- Glutamine synthetase activity in leaves of Zea mays L. as influenced by magnesium status.Planta · 2015Article
- Mineral nitrogen sources differently affect root glutamine synthetase isoforms and amino acid balance among organs in maize.BMC plant biology · 2015Article
- Glutamine synthetase in Medicago truncatula, unveiling new secrets of a very old enzyme.Frontiers in plant science · 2015Review
- Novel aspects of glutamine synthetase (GS) regulation revealed by a detailed expression analysis of the entire GS gene family of Medicago truncatula under different physiological conditions.BMC plant biology · 2013Article
- 14-3-3 proteins SGF14c and SGF14l play critical roles during soybean nodulation.Plant physiology · 2012Article
- Glutamine synthetase in legumes: recent advances in enzyme structure and functional genomics.International journal of molecular sciences · 2012Review
- Medicago PhosphoProtein Database: a repository for Medicago truncatula phosphoprotein data.Frontiers in plant science · 2012Article
- Determining novel functions of Arabidopsis 14-3-3 proteins in central metabolic processes.BMC systems biology · 2011Article
- Glutamine synthetase is a molecular target of nitric oxide in root nodules of Medicago truncatula and is regulated by tyrosine nitration.Plant physiology · 2011Article
- Medicago truncatula contains a second gene encoding a plastid located glutamine synthetase exclusively expressed in developing seeds.BMC plant biology · 2010Article
- Large-scale phosphoprotein analysis in Medicago truncatula roots provides insight into in vivo kinase activity in legumes.Plant physiology · 2010Article
- Proteomic profiling of tandem affinity purified 14-3-3 protein complexes in Arabidopsis thaliana.Proteomics · 2009Article
- Two cytosolic glutamine synthetase isoforms of maize are specifically involved in the control of grain production.The Plant cell · 2006Article
- Signalling and regulation of plant development by carbon/nitrogen balance.Physiologia plantarumReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this report we demonstrate that plastid glutamine synthetase of Medicago truncatula (MtGS2) is regulated by phosphorylation and 14-3-3 interaction. To investigate regulatory aspects of GS2 phosphorylation, we have produced non-phosphorylated GS2 proteins by expressing the plant cDNA in E. coli and performed in vitro phosphorylation assays. The recombinant isoenzyme was phosphorylated by calcium dependent kinase(s) present in leaves, roots and nodules. Using an (His)6-tagged 14-3-3 protein column affinity purification method, we demonstrate that phosphorylated GS2 interacts with 14-3-3 proteins and that this interaction leads to selective proteolysis of the plastid located isoform, resulting in inactivation of the isoenzyme. By site directed mutagenesis we were able to identify a GS2 phosphorylation site (Ser97) crucial for the interaction with 14-3-3s. Phosphorylation of this target residue can be functionally mimicked by replacing Ser97 by Asp, indicating that the introduction of a negative charge contributes to the interaction with 14-3-3 proteins and subsequent specific proteolysis. Furthermore, we document that plant extracts contain protease activity that cleaves the GS2 protein only when it is bound to 14-3-3 proteins following either phosphorylation or mimicking of phosphorylation by Ser97Asp.
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