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Boutonnet, M.

Publications and source records attributed to Boutonnet, M..

3 recordsLinked to original sources

CNIH3 is a molecular signature of slow AMPA receptors

At excitatory synapses, glutamate activates receptors in the postsynaptic membrane including the AMPA receptor. Usually considered to be the fastest ion channel receptors in the brain, AMPA receptors can produce millisecond synaptic potentials that mimic the timing of spikes. However, we found abundant slow AMPA responses in CA1 pyramidal cells. These slow responses show a mosaic distribution in individual cells and even in single dendrites (Pampaloni et al., 2021). A survey of the literature reveals cryptic reports of similar slow responses in cerebellum, striatum and other brain regions (Pampaloni and Plested, 2022). These observations open a new perspective on the extent of AMPA receptor diversity. To enable a detailed interrogation of slow AMPA receptors in the brain, we sought to determine their molecular basis. We noted that slow AMPA is prevalent in ventral CA1 but rather sparse in dorsal hippocampus and absent in dentate gyrus granule cells. Checking published transcriptomic data, we noted that certain AMPA receptor auxiliary proteins also show gradients across these hippocampal regions. One understudied auxiliary protein identified from transcriptomics, CNIH3, produces uniquely slow AMPA responses in heterologous expression. Strikingly, we found that shRNAs against CNIH3 could ablate slow AMPA responses in ventral CA1, and over-expression of CNIH3 in dorsal CA1 introduced widespread mosaic slow AMPA responses. We conclude that CNIH3 is a sparsely-expressed marker of slow AMPA currents with the potential to convert individual synapses from fast followers into detonators that can spike the target cell, with implications for subcellular calculations, circuits, behaviour and brain pathologies.

neuroscience↗

The gut microbiota-derived metabolite queuosine regulates neuronal development and network function through tRNA modification

Queuosine (Q) modification is a hypermodified nucleoside derived from guanine on tRNAs that enhances the decoding of codons and equilibrates translational speed. Q is biosynthesized in bacteria, and eukaryotes salvage Q and the nucleobase queuine from the diet and the gut microbiome. In animals, Q deficiency causes impaired proteostasis, mitochondrial dysfunction, and neurological phenotypes, possibly due to the longevity and high metabolic demand of neurons. Yet, how Q affects isolated neurons has not been explored yet. Here, primary rat cortical neurons were cultured in Q-free synthetic medium to directly modulate Q modification levels independently of genetic perturbation, enabling assessment of its effects on neuronal development, survival, morphology, synaptic organization, and activity. Importantly, we found that the presence of Q modification facilitated neuronal arborization, decreased inhibitory synaptic density, and increased the frequency of spontaneous calcium transients, showing that tRNA Q modification enhances neuronal structural maturation and synaptic activity. Thus, the fine-tuning of neuronal translation programs by Q-tRNAs is required for proper network development and may influence neuronal resilience and synaptic function.

neuroscience↗

Voltage tunes mGlu5 receptor function, impacting synaptic transmission

Voltage sensitivity is a common feature of many membrane proteins, including some G-protein coupled receptors (GPCRs). However, the functional consequences of voltage sensitivity in GPCRs are not well understood. In this study, we investigated the voltage sensitivity of the post-synaptic metabotropic glutamate receptor mGlu5 and its impact on synaptic transmission. Using biosensors and electrophysiological recordings in non-excitable HEK293T cells or neurons, we found that mGlu5 receptor function is optimal at resting membrane potentials. We observed that membrane depolarization significantly reduced mGlu5 receptor activation, Gq-PLC/PKC stimulation, Ca2+ release, and mGlu5 receptor-gated currents through TRPC6 channels or NMDA receptors. Notably, we report a previously unknown activity of the NMDA receptor at the resting potential of neurons, enabled by mGlu5. Our findings suggest that mGlu5 receptor activity is directly regulated by membrane voltage which may have a significant impact on synaptic processes and pathophysiological functions.

neuroscience↗