A Frameshift Variant of GluN2A Identified in an Epilepsy Patient Results in NMDA Receptor Mistargeting

突触后密度 突触后电位 NMDA受体 神经科学 生物 树突棘 谷氨酸受体 神经传递 突触 突触可塑性 细胞生物学 受体 遗传学 海马结构
作者
Marta Vieira,Shiyong Peng,Seong Hyun Won,Eun‐Hye Hong,Sara K. Inati,Audrey Thurm,A. H. Thiam,Sarah Kim-Hellmuth,Sarah J. Myers,John Badger,Stephen F. Traynelis,Wei Lü,K. W. Roche
出处
期刊:The Journal of Neuroscience [Society for Neuroscience]
卷期号:44 (4): e0557232023-e0557232023 被引量:2
标识
DOI:10.1523/jneurosci.0557-23.2023
摘要

N -methyl- D -aspartate receptors (NMDARs) are crucial for neuronal development and synaptic plasticity. Dysfunction of NMDARs is associated with multiple neurodevelopmental disorders, including epilepsy, autism spectrum disorder, and intellectual disability. Understanding the impact of genetic variants of NMDAR subunits can shed light on the mechanisms of disease. Here, we characterized the functional implications of a de novo mutation of the GluN2A subunit (P1199Rfs*32) resulting in the truncation of the C-terminal domain. The variant was identified in a male patient with epileptic encephalopathy, multiple seizure types, severe aphasia, and neurobehavioral changes. Given the known role of the CTD in NMDAR trafficking, we examined changes in receptor localization and abundance at the postsynaptic membrane using a combination of molecular assays in heterologous cells and rat primary neuronal cultures. We observed that the GluN2A P1199Rfs*32-containing receptors traffic efficiently to the postsynaptic membrane but have increased extra-synaptic expression relative to WT GluN2A-containing NMDARs. Using in silico predictions, we hypothesized that the mutant would lose all PDZ interactions, except for the recycling protein Scribble1. Indeed, we observed impaired binding to the scaffolding protein postsynaptic protein-95 (PSD-95); however, we found the mutant interacts with Scribble1, which facilitates the recycling of both the mutant and the WT GluN2A. Finally, we found that neurons expressing GluN2A P1199Rfs*32 have fewer synapses and decreased spine density, indicating compromised synaptic transmission in these neurons. Overall, our data show that GluN2A P1199Rfs*32 is a loss-of-function variant with altered membrane localization in neurons and provide mechanistic insight into disease etiology.
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