An unexpected role for a glutamate receptor

• 成果类型: Editorial Material
• 署名作者: Coombs, Ian D.; Farrant, Mark
• 署名单位: University of London; University College London
• 刊物名称: SCIENCE
• ISSN/ISSBN: 0036-10230
• DOI: 10.1126/science.adm6771
• 发表日期: 2023-12-22
• 页码: 1363-1364
• 关键词: delta-2

摘要

Ion channels activated by the neurotransmitter glutamate underlie excitatory signaling between neurons in the brain. In mammals, these ionotropic glutamate receptors (iGluRs) belong to three families formed from GluA, GluN, and GluK subunits, respectively: the alpha-amino-3-hydroxy- 5-methyl-4-isoxazolepropionic acid (AMPA), N-methyl-D-aspartate (NMDA), and kainate receptors (1). By contrast, receptors of a fourth homologous iGluR family-the delta or GluD receptors-do not respond to glutamate. Despite sharing a similar architecture with other iGluRs, including a transmembrane pore, the question of whether GluD receptors pass current has been controversial (2, 3). Instead, they are best known as synaptic organizing proteins (2, 4). On page 1389 of this issue, Piot et al. (5) show that one GluD family member, GluD1, can bind the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) and trigger potentiation of GABA-mediated synaptic currents. This challenges the dogmatic distinction between glutamate and GABA receptors and identifies GluD1 as a regulator of inhibitory signaling.