8bn2
From Proteopedia
Crystal structure of the ligand-binding domain (LBD) of human iGluR Delta-1 (GluD1) in complex with D-Serine
Structural highlights
FunctionGRID1_HUMAN Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. Publication Abstract from PubMedFast synaptic neurotransmission in the vertebrate central nervous system relies primarily on ionotropic glutamate receptors (iGluRs), which drive neuronal excitation, and type A gamma-aminobutyric acid receptors (GABA(A)Rs), which are responsible for neuronal inhibition. However, the GluD1 receptor, an iGluR family member, is present at both excitatory and inhibitory synapses. Whether and how GluD1 activation may affect inhibitory neurotransmission is unknown. In this work, by using a combination of biochemical, structural, and functional analyses, we demonstrate that GluD1 binds GABA, a previously unknown feature of iGluRs. GluD1 activation produces long-lasting enhancement of GABAergic synaptic currents in the adult mouse hippocampus through a non-ionotropic mechanism that is dependent on trans-synaptic anchoring. The identification of GluD1 as a GABA receptor that controls inhibitory synaptic plasticity challenges the classical dichotomy between glutamatergic and GABAergic receptors. GluD1 binds GABA and controls inhibitory plasticity.,Piot L, Heroven C, Bossi S, Zamith J, Malinauskas T, Johnson C, Wennagel D, Stroebel D, Charrier C, Aricescu AR, Mony L, Paoletti P Science. 2023 Dec 22;382(6677):1389-1394. doi: 10.1126/science.adf3406. Epub 2023 , Dec 7. PMID:38060673[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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