ArticleCellular and molecular life sciences : CMLS2025
D-Serine disrupts Cbln1 and GluD1 interaction and affects Cbln1-dependent synaptic effects and nocifensive responses in the central amygdala.
Article in Cellular and molecular life sciences : CMLS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- GluD1 is localized at cholinergic synapses and is an acetylcholine receptor.Molecular psychiatry · 2026Article
- GluD1 at the synaptic crossroads: from domain structure to circuit dysfunction.Acta pharmacologica Sinica · 2026Review
- D-serine: A Multitalented Neuromodulator in Brain Function, Systemic Homeostasis, and Disease.Cellular and molecular neurobiology · 2026Review
- Glutamate Delta 1 Receptor in Synapses, Circuits, and Disease.The European journal of neuroscience · 2026Review
- Deletion of Glutamate Delta 1 Receptor Leads to Heterogeneous Transcription and Synaptic Gene Alterations Across Brain Regions.International journal of molecular sciences · 2025Article
- Promoter demethylation of cerebellin 2 by ten-eleven translocation 3 contributes to peripheral sensitization in trigeminal neuropathic pain of mice.The journal of headache and pain · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Ionotropic glutamate receptors (iGluRs) mediate fast excitatory neurotransmission in the nervous system. In addition to NMDA receptor co-agonists, D-serine is a ligand for glutamate delta receptors (GluDs) and interacts with the ligand-binding domain with low affinity. However, D-serine binding does not lead to typical ion channel currents in GluD1 or GluD2 but may contribute to synaptic plasticity. In the developing brain, D-serine binding to GluD2 facilitates long-term depression at parallel fiber-Purkinje cell synapses. However, the influence of D-serine on GluD1's interaction with its amino terminal domain synaptogenic ligand Cbln1 and its subsequent impact on synaptic function and behavior remains unexplored. Here, we found that D-serine inhibited the interaction between Cbln1 and GluD1 in an in vitro cell-binding assay. This effect was concentration-dependent, with an IC
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Registered trials
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