ArticleThe Journal of biological chemistry2011
Effect of Src kinase phosphorylation on disordered C-terminal domain of N-methyl-D-aspartic acid (NMDA) receptor subunit GluN2B protein.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 46 citations in OpenAlex.
- Differences in Src phosphorylation of PSD-93 and PSD-95 drive differences in scaffolding activity.Protein science : a publication of the Protein Society · 2026Article
- Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023Review
- Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology.Biomolecules · 2023Review
- Different Forms of Disorder in NMDA-Sensitive Glutamate Receptor Cytoplasmic Domains Are Associated with Differences in Condensate Formation.Biomolecules · 2022Article
- Regulation of the NMDA receptor by its cytoplasmic domains: (How) is the tail wagging the dog?Neuropharmacology · 2021Review
- Article
- Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules.Micromachines · 2021Review
- Structural Dynamics of Glutamate Signaling Systems by smFRET.Biophysical journal · 2020Review
- Specific Conformational Dynamics and Expansion Underpin a Multi-Step Mechanism for Specific Binding of p27 with Cdk2/Cyclin A.Journal of molecular biology · 2020Article
- Single-molecule fluorescence studies of intrinsically disordered proteins and liquid phase separation.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- Spontaneous Switching among Conformational Ensembles in Intrinsically Disordered Proteins.Biomolecules · 2019Review
- Phosphorylation Induces Conformational Rigidity at the C-Terminal Domain of AMPA Receptors.The journal of physical chemistry. B · 2019Article
- NMDA receptor C-terminal signaling in development, plasticity, and disease.F1000Research · 2019Review
- Single Molecule FRET: A Powerful Tool to Study Intrinsically Disordered Proteins.Biomolecules · 2018Review
- Functions of intrinsic disorder in transmembrane proteins.Cellular and molecular life sciences : CMLS · 2017Review
- Conformational change of syntaxin linker region induced by Munc13s initiates SNARE complex formation in synaptic exocytosis.The EMBO journal · 2017Article
- Modulation of NMDA channel gating by CaScientific reports · 2016Article
- Behavioral and physiological characterization of PKC-dependent phosphorylation in the Grin2a∆PKC mouse.Brain research · 2016Article
- Src Family Kinases in Brain Edema After Acute Brain Injury.Acta neurochirurgica. Supplement · 2016Article
- A structural biology perspective on NMDA receptor pharmacology and function.Current opinion in structural biology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
NMDA receptors are ligand-gated ion channels with a regulatory intracellular C-terminal domain (CTD). In GluN2B, the CTD is the largest domain in the protein but is intrinsically disordered. The GluN2B subunit is the major tyrosine-phosphorylated protein in synapses. Src kinase phosphorylates the GluN2B CTD, but it is unknown how this affects channel activity. In disordered proteins, phosphorylation can tip the balance between order and disorder. Transitions can occur in both directions, so it is not currently possible to predict the effects of phosphorylation. We used single molecule fluorescence to characterize the effects of Src phosphorylation on GluN2B. Scanning fluorescent labeling sites throughout the domain showed no positional dependence of the energy transfer. Instead, efficiency only scaled with the separation between labeling sites suggestive of a relatively featureless conformational energy landscape. Src phosphorylation led to a general expansion of the polypeptide, which would result in greater exposure of known protein-binding sites and increase the physical separation between contiguous sites. Phosphorylation makes the CTD more like a random coil leaving open the question of how Src exerts its effects on the NMDA receptor.
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What OpenQuestion holds
Registered trials
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.